Relevant bibliographies by topics / Zinc fingers

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Academic literature on the topic 'Zinc fingers'

Author: Grafiati
Published: 4 June 2021
Last updated: 15 June 2025

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Journal articles on the topic "Zinc fingers"

1

Keller, A. D., and T. Maniatis. "Only two of the five zinc fingers of the eukaryotic transcriptional repressor PRDI-BF1 are required for sequence-specific DNA binding." Molecular and Cellular Biology 12, no. 5 (1992): 1940–49. http://dx.doi.org/10.1128/mcb.12.5.1940-1949.1992.

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The eukaryotic transcriptional repressor PRDI-BF1 contains five zinc fingers of the C2H2 type, and the protein binds specifically to PRDI, a 14-bp regulatory element of the beta interferon gene promoter. We have investigated the amino acid sequence requirements for specific binding to PRDI and found that the five zinc fingers and a short stretch of amino acids N terminal to the first finger are necessary and sufficient for PRDI-specific binding. The contribution of individual zinc fingers to DNA binding was investigated by inserting them in various combinations into another zinc finger-containing DNA-binding protein whose own fingers had been removed. We found that insertion of PRDI-BF1 zinc fingers 1 and 2 confer PRDI-binding activity on the recipient protein. In contrast, the insertion of PRDI-BF1 zinc fingers 2 through 5, the insertion of zinc finger 1 or 2 alone, and the insertion of zinc fingers 1 and 2 in reverse order did not confer PRDI-binding activity. We conclude that the first two PRDI-BF1 zinc fingers together are sufficient for the sequence-specific recognition of PRDI.
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Keller, A. D., and T. Maniatis. "Only two of the five zinc fingers of the eukaryotic transcriptional repressor PRDI-BF1 are required for sequence-specific DNA binding." Molecular and Cellular Biology 12, no. 5 (1992): 1940–49. http://dx.doi.org/10.1128/mcb.12.5.1940.

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The eukaryotic transcriptional repressor PRDI-BF1 contains five zinc fingers of the C2H2 type, and the protein binds specifically to PRDI, a 14-bp regulatory element of the beta interferon gene promoter. We have investigated the amino acid sequence requirements for specific binding to PRDI and found that the five zinc fingers and a short stretch of amino acids N terminal to the first finger are necessary and sufficient for PRDI-specific binding. The contribution of individual zinc fingers to DNA binding was investigated by inserting them in various combinations into another zinc finger-containing DNA-binding protein whose own fingers had been removed. We found that insertion of PRDI-BF1 zinc fingers 1 and 2 confer PRDI-binding activity on the recipient protein. In contrast, the insertion of PRDI-BF1 zinc fingers 2 through 5, the insertion of zinc finger 1 or 2 alone, and the insertion of zinc fingers 1 and 2 in reverse order did not confer PRDI-binding activity. We conclude that the first two PRDI-BF1 zinc fingers together are sufficient for the sequence-specific recognition of PRDI.
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GREEN, Andrew, and Bibudhendra SARKAR. "Alteration of zif268 zinc-finger motifs gives rise to non-native zinc-co-ordination sites but preserves wild-type DNA recognition." Biochemical Journal 333, no. 1 (1998): 85–90. http://dx.doi.org/10.1042/bj3330085.

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Zinc fingers are among the major structural motifs found in proteins that are involved in eukaryotic gene regulation. Many of these zinc-finger domains are involved in DNA binding. This study investigated whether the zinc-co-ordinating (Cys)2(His)2 motif found in the three zinc fingers of zif268 could be replaced by a (Cys)4 motif while still preserving DNA recognition. (Cys)2(His)2-to-(Cys)4 mutations were generated in each of the three zinc fingers of zif268 individually, as well as in fingers 1 and 3, and fingers 2 and 3 together. Whereas finger 1 and finger 3 tolerate the switch, such an alteration in finger 2 renders the polypeptide incapable of DNA recognition. The protein–DNA interaction was examined in greater detail by using a methylation-interference assay. The mutant polypeptides containing the (Cys)4 motif in fingers 1 or 3 recognize DNA in a manner identical to the wild-type protein, suggesting that the (Cys)4 motif appears to give rise to a properly folded finger. Additional results indicate that a zif268 variant containing a (Cys)2(His)(Ala) arrangement in finger 1 is also capable of DNA recognition in a manner identical to the wild-type polypeptide. This appears to be the first time that such alterations, in the context of an intact DNA-binding domain, have still allowed for specific DNA recognition. Taken together, the work presented here enhances our understanding of the relationship between metal ligation and DNA-binding by zinc fingers.
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Drummond, I. A., H. D. Rupprecht, P. Rohwer-Nutter, et al. "DNA recognition by splicing variants of the Wilms' tumor suppressor, WT1." Molecular and Cellular Biology 14, no. 6 (1994): 3800–3809. http://dx.doi.org/10.1128/mcb.14.6.3800-3809.1994.

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The Wilms' tumor suppressor, WT1, is a zinc finger transcriptional regulator which exists as multiple forms owing to alternative mRNA splicing. The most abundant splicing variants contain a nine-nucleotide insertion encoding lysine, threonine, and serine (KTS) in the H-C link region between the third and fourth WT1 zinc fingers which disrupts binding to a previously defined WT1-EGR1 binding site. We have identified WT1[+KTS] binding sites in the insulin-like growth factor II gene and show that WT1[+KTS] represses transcription from the insulin-like growth factor II P3 promoter. The highest affinity WT1[+KTS] DNA binding sites included nucleotide contacts involving all four WT1 zinc fingers. We also found that different subsets of three WT1 zinc fingers could bind to distinct DNA recognition elements. A tumor-associated, WT1 finger 3 deletion mutant was shown to bind to juxtaposed nucleotide triplets for the remaining zinc fingers 1, 2, and 4. The characterization of novel WT1 DNA recognition elements adds a new level of complexity to the potential gene regulatory activity of WT1. The results also present the possibility that altered DNA recognition by the dominant WT1 zinc finger 3 deletion mutant may contribute to tumorigenesis.
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Drummond, I. A., H. D. Rupprecht, P. Rohwer-Nutter, et al. "DNA recognition by splicing variants of the Wilms' tumor suppressor, WT1." Molecular and Cellular Biology 14, no. 6 (1994): 3800–3809. http://dx.doi.org/10.1128/mcb.14.6.3800.

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The Wilms' tumor suppressor, WT1, is a zinc finger transcriptional regulator which exists as multiple forms owing to alternative mRNA splicing. The most abundant splicing variants contain a nine-nucleotide insertion encoding lysine, threonine, and serine (KTS) in the H-C link region between the third and fourth WT1 zinc fingers which disrupts binding to a previously defined WT1-EGR1 binding site. We have identified WT1[+KTS] binding sites in the insulin-like growth factor II gene and show that WT1[+KTS] represses transcription from the insulin-like growth factor II P3 promoter. The highest affinity WT1[+KTS] DNA binding sites included nucleotide contacts involving all four WT1 zinc fingers. We also found that different subsets of three WT1 zinc fingers could bind to distinct DNA recognition elements. A tumor-associated, WT1 finger 3 deletion mutant was shown to bind to juxtaposed nucleotide triplets for the remaining zinc fingers 1, 2, and 4. The characterization of novel WT1 DNA recognition elements adds a new level of complexity to the potential gene regulatory activity of WT1. The results also present the possibility that altered DNA recognition by the dominant WT1 zinc finger 3 deletion mutant may contribute to tumorigenesis.
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Heller, Jennifer, Hilde Schjerven, Ju Qiu, Aileen Lee, Stephen Smale, and Liang Zhou. "Selective requirement of Ikaros zinc fingers in Treg and Th17 fate decision. (P1137)." Journal of Immunology 190, no. 1_Supplement (2013): 50.11. http://dx.doi.org/10.4049/jimmunol.190.supp.50.11.

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Abstract TGF-β is a common factor important for the differentiation of pro-inflammatory Th17 and anti-inflammatory inducible Treg cells. However, the precise molecular mechanisms underlying the fate decision of differentiating CD4+ T cells in the presence of TGF-β is poorly understood. Here, we show that distinctive N-terminal DNA-binding zinc fingers of Ikaros play essential roles in Treg and Th17 fate decision. Ikaros has a highly conserved DNA-binding domain near the N-terminus with four tandem zinc fingers. Zinc fingers 2 and 3 are required for stable binding to DNA, whereas fingers 1 and 4 appear to be important for differentially modulating binding properties to specific sites at target genes. Our data show that T cells lacking Ikaros zinc finger 4 but not 1 failed to differentiate into Foxp3+ Tregs upon TGF-β stimulation. Instead, TGF-β-skewed Ikaros zinc finger 4 mutant cells displayed aberrant upregulation of Th17-associated cytokines IL-17 and IL-22. IL-17 but not IL-22 upregulation is dependent on transcription factor RORγt. Aryl hydrocarbon receptor, an essential transcription factor required for IL-22 expression, was unexpectedly decreased. Together, our data uncover a novel selective requirement for Ikaros zinc fingers in the differentiation of Treg and Th17 cells and an intricate interplay among various transcription factors in programming Th17/Treg lineages. We are currently examining the role of Ikaros zinc finger 4 in infection and autoimmunity.
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Li, Yong, Tomoki Kimura, John H. Laity, and Glen K. Andrews. "The Zinc-Sensing Mechanism of Mouse MTF-1 Involves Linker Peptides between the Zinc Fingers." Molecular and Cellular Biology 26, no. 15 (2006): 5580–87. http://dx.doi.org/10.1128/mcb.00471-06.

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ABSTRACT Mouse metal response element-binding transcription factor-1 (MTF-1) regulates the transcription of genes in response to a variety of stimuli, including exposure to zinc or cadmium, hypoxia, and oxidative stress. Each of these stresses may increase labile cellular zinc, leading to nuclear translocation, DNA binding, and transcriptional activation of metallothionein genes (MT genes) by MTF-1. Several lines of evidence suggest that the highly conserved six-zinc finger DNA-binding domain of MTF-1 also functions as a zinc-sensing domain. In this study, we investigated the potential role of the peptide linkers connecting the four N-terminal zinc fingers of MTF-1 in their zinc-sensing function. Each of these three linkers is unique, completely conserved among all known vertebrate MTF-1 orthologs, and different from the canonical Cys2His2 zinc finger TGEKP linker sequence. Replacing the RGEYT linker between zinc fingers 1 and 2 with TGEKP abolished the zinc-sensing function of MTF-1, resulting in constitutive DNA binding, nuclear translocation, and transcriptional activation of the MT-I gene. In contrast, swapping the TKEKP linker between fingers 2 and 3 with TGEKP had little effect on the metal-sensing functions of MTF-1, whereas swapping the canonical linker for the shorter TGKT linker between fingers 3 and 4 rendered MTF-1 less sensitive to zinc-dependent activation both in vivo and in vitro. These observations suggest a mechanism by which physiological concentrations of accessible cellular zinc affect MTF-1 activity. Zinc may modulate highly specific, linker-mediated zinc finger interactions in MTF-1, thus affecting its zinc- and DNA-binding activities, resulting in translocation to the nucleus and binding to the MT-I gene promoter.
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Morris, J. F., R. Hromas, and F. J. Rauscher. "Characterization of the DNA-binding properties of the myeloid zinc finger protein MZF1: two independent DNA-binding domains recognize two DNA consensus sequences with a common G-rich core." Molecular and Cellular Biology 14, no. 3 (1994): 1786–95. http://dx.doi.org/10.1128/mcb.14.3.1786-1795.1994.

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The myeloid zinc finger gene 1, MZF1, encodes a transcription factor which is expressed in hematopoietic progenitor cells that are committed to myeloid lineage differentiation. MZF1 contains 13 C2H2 zinc fingers arranged in two domains which are separated by a short glycine- and proline-rich sequence. The first domain consists of zinc fingers 1 to 4, and the second domain is formed by zinc fingers 5 to 13. We have determined that both sets of zinc finger domains bind DNA. Purified, recombinant MZF1 proteins containing either the first set of zinc fingers or the second set were prepared and used to affinity select DNA sequences from a library of degenerate oligonucleotides by using successive rounds of gel shift followed by PCR amplification. Surprisingly, both DNA-binding domains of MZF1 selected similar DNA-binding consensus sequences containing a core of four or five guanine residues, reminiscent of an NF-kappa B half-site: 1-4, 5'-AGTGGGGA-3'; 5-13, 5'-CGGGnGAGGGGGAA-3'. The full-length MZF1 protein containing both sets of zinc finger DNA-binding domains recognizes synthetic oligonucleotides containing either the 1-4 or 5-13 consensus binding sites in gel shift assays. Thus, we have identified the core DNA consensus binding sites for each of the two DNA-binding domains of a myeloid-specific zinc finger transcription factor. Identification of these DNA-binding sites will allow us to identify target genes regulated by MZF1 and to assess the role of MZF1 as a transcriptional regulator of hematopoiesis.
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Morris, J. F., R. Hromas, and F. J. Rauscher. "Characterization of the DNA-binding properties of the myeloid zinc finger protein MZF1: two independent DNA-binding domains recognize two DNA consensus sequences with a common G-rich core." Molecular and Cellular Biology 14, no. 3 (1994): 1786–95. http://dx.doi.org/10.1128/mcb.14.3.1786.

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The myeloid zinc finger gene 1, MZF1, encodes a transcription factor which is expressed in hematopoietic progenitor cells that are committed to myeloid lineage differentiation. MZF1 contains 13 C2H2 zinc fingers arranged in two domains which are separated by a short glycine- and proline-rich sequence. The first domain consists of zinc fingers 1 to 4, and the second domain is formed by zinc fingers 5 to 13. We have determined that both sets of zinc finger domains bind DNA. Purified, recombinant MZF1 proteins containing either the first set of zinc fingers or the second set were prepared and used to affinity select DNA sequences from a library of degenerate oligonucleotides by using successive rounds of gel shift followed by PCR amplification. Surprisingly, both DNA-binding domains of MZF1 selected similar DNA-binding consensus sequences containing a core of four or five guanine residues, reminiscent of an NF-kappa B half-site: 1-4, 5'-AGTGGGGA-3'; 5-13, 5'-CGGGnGAGGGGGAA-3'. The full-length MZF1 protein containing both sets of zinc finger DNA-binding domains recognizes synthetic oligonucleotides containing either the 1-4 or 5-13 consensus binding sites in gel shift assays. Thus, we have identified the core DNA consensus binding sites for each of the two DNA-binding domains of a myeloid-specific zinc finger transcription factor. Identification of these DNA-binding sites will allow us to identify target genes regulated by MZF1 and to assess the role of MZF1 as a transcriptional regulator of hematopoiesis.
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Klug, Aaron, and John W. R. Schwabe. "Zinc fingers." FASEB Journal 9, no. 8 (1995): 597–604. http://dx.doi.org/10.1096/fasebj.9.8.7768350.

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Dissertations / Theses on the topic "Zinc fingers"

1

Blancafort, Pilar. "Making conformation-specific RNA-binding zinc fingers." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0023/NQ47598.pdf.

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2

Giesecke, Astrid. "Protein-protein interactions mediated by Cys2His2 zinc-fingers." [S.l.] : [s.n.], 2006. http://deposit.ddb.de/cgi-bin/dokserv?idn=981809715.

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Isalan, Mark David. "Selection of zinc fingers with novel DNA-binding specificities." Thesis, University of Cambridge, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.621667.

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Looman, Camilla. "The ABC of KRAB zinc finger proteins." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis : Univ.-bibl. [distributör], 2003. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-3515.

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Hallal, Samantha. "Characterisation of the zinc fingers of erythroid krüppel-like factor." Connect to full text, 2008. http://ses.library.usyd.edu.au/handle/2123/4030.

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Thesis (Ph. D.)--University of Sydney, 2009.<br>Title from title screen (viewed February 10, 2009). Submitted in fulfilment of the requirements for the degree of Doctor of Philosophy to the School of Molecular and Microbial Biosciences, Faculty of Science. Degree awarded 2009; thesis submitted 2008. Includes bibliographical references. Also available in print form.
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Hallal, Samantha. "Characterisation of the zinc fingers of Erythroid Kruppel-Like Factor." Thesis, The University of Sydney, 2008. http://hdl.handle.net/2123/4030.

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Gene expression is known to be regulated at the level of transcription. Recently, however, there has been a growing realisation of the importance of gene regulation at the post-transcriptional level, namely at the level of pre-mRNA processing (5’ capping, splicing and polyadenylation), nuclear export, mRNA localisation and translation. Erythroid krüppel-like factor (Eklf) is the founding member of the Krüppel-like factor (Klf) family of transcription factors and plays an important role in erythropoiesis. In addition to its nuclear presence, Eklf was recently found to localise to the cytoplasm and this observation prompted us to examine whether this protein has a role as an RNA-binding protein, in addition to its well-characterised DNA-binding function. In this thesis we demonstrate that Eklf displays RNA-binding activity in an in vitro and in vivo context through the use of its classical zinc finger (ZF) domains. Furthermore, using two independent in vitro assays, we show that Eklf has a preference for A and U RNA homoribopolymers. These results represent the first description of RNA-binding by a member of the Klf family. We developed a dominant negative mutant of Eklf by expressing its ZF region in murine erythroleukaemia (MEL) cells. We used this to investigate the importance of this protein in haematopoietic lineage decisions by examining its effect on the multipotent K562 cell line. We provide evidence that Eklf appears to be critical not only for the promotion of erythropoiesis, but also for the inhibition of megakaryopoiesis.
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Hallal, Samantha. "Characterisation of the zinc fingers of Erythroid Kruppel-Like Factor." University of Sydney, 2008. http://hdl.handle.net/2123/4030.

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Doctor of Philosophy (PhD)<br>Gene expression is known to be regulated at the level of transcription. Recently, however, there has been a growing realisation of the importance of gene regulation at the post-transcriptional level, namely at the level of pre-mRNA processing (5’ capping, splicing and polyadenylation), nuclear export, mRNA localisation and translation. Erythroid krüppel-like factor (Eklf) is the founding member of the Krüppel-like factor (Klf) family of transcription factors and plays an important role in erythropoiesis. In addition to its nuclear presence, Eklf was recently found to localise to the cytoplasm and this observation prompted us to examine whether this protein has a role as an RNA-binding protein, in addition to its well-characterised DNA-binding function. In this thesis we demonstrate that Eklf displays RNA-binding activity in an in vitro and in vivo context through the use of its classical zinc finger (ZF) domains. Furthermore, using two independent in vitro assays, we show that Eklf has a preference for A and U RNA homoribopolymers. These results represent the first description of RNA-binding by a member of the Klf family. We developed a dominant negative mutant of Eklf by expressing its ZF region in murine erythroleukaemia (MEL) cells. We used this to investigate the importance of this protein in haematopoietic lineage decisions by examining its effect on the multipotent K562 cell line. We provide evidence that Eklf appears to be critical not only for the promotion of erythropoiesis, but also for the inhibition of megakaryopoiesis.
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Simpson, Raina Jui Yu. "The multiple roles of zinc finger domains." Thesis, The University of Sydney, 2004. http://hdl.handle.net/2123/655.

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Zinc finger (ZnF) domains are prevalent in eukaryotes and play crucial roles in mediating protein-DNA and protein-protein interactions. This Thesis focuses on the molecular details underlying interactions mediated by two ZnF domains. The GATA-1 protein is vital for the development of erythrocytes and megakaryocytes. Pertinent to the protein function is the N-terminal ZnF. In particular, this domain mediates interaction with DNA containing GATC motifs and the coactivator protein FOG. The importance of these interactions was illustrated by the findings in Chapter 3 that naturally occurring mutations identified in patients suffering from blood disorders affect the interaction of the N-terminal ZnF with either DNA (R216Q mutation) or FOG (V205M and G208S mutations). In addition to the interaction FOG makes with GATA-1, it also interacts with the centrosomal protein TACC3. In Chapter 4, this interaction is characterised in detail. The solution structure of the region of FOG responsible for the interaction is determined using NMR spectroscopy, revealing that it is a true classical zinc finger, and characterisation of the interaction domain of TACC3 showed that the region is a dimeric coiled-coil. The FOG:TACC3 interaction appears to be mediated by a-helices from the two proteins. The data presented here represent some of the first described molecular details of how a classical ZnF can contact a protein partner. Interestingly, the a-helix used by the FOG finger to bind TACC3 is the same region utilised by DNA-binding classical zinc fingers to contact DNA. In addition to the multiple roles played by ZnFs, this domain is also known for its robustness and versatility. In Chapter 5, incomplete ZnF sequences were assessed for its ability to form functional zinc-binding domains. Remarkably, CCHX sequences (in the context of BKLF finger 3) were able to form discrete zinc-binding domains and also, mediate both protein-DNA and protein-protein interactions. This result not only illustrates the robust nature of ZnFs, it highlights the need for expanding ZnF sequence criteria when searching for functional zinc-binding modules. Together, the data presented here help further our understanding of zinc finger domains. Similar to the use of DNA-binding ZnFs in designer proteins, these data may start us on the path of designing novel protein-binding ZnFs.
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Simpson, Raina Jui Yu. "The multiple roles of zinc finger domains." University of Sydney. Molecular and Microbial Biosciences, 2004. http://hdl.handle.net/2123/655.

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Zinc finger (ZnF) domains are prevalent in eukaryotes and play crucial roles in mediating protein-DNA and protein-protein interactions. This Thesis focuses on the molecular details underlying interactions mediated by two ZnF domains. The GATA-1 protein is vital for the development of erythrocytes and megakaryocytes. Pertinent to the protein function is the N-terminal ZnF. In particular, this domain mediates interaction with DNA containing GATC motifs and the coactivator protein FOG. The importance of these interactions was illustrated by the findings in Chapter 3 that naturally occurring mutations identified in patients suffering from blood disorders affect the interaction of the N-terminal ZnF with either DNA (R216Q mutation) or FOG (V205M and G208S mutations). In addition to the interaction FOG makes with GATA-1, it also interacts with the centrosomal protein TACC3. In Chapter 4, this interaction is characterised in detail. The solution structure of the region of FOG responsible for the interaction is determined using NMR spectroscopy, revealing that it is a true classical zinc finger, and characterisation of the interaction domain of TACC3 showed that the region is a dimeric coiled-coil. The FOG:TACC3 interaction appears to be mediated by a-helices from the two proteins. The data presented here represent some of the first described molecular details of how a classical ZnF can contact a protein partner. Interestingly, the a-helix used by the FOG finger to bind TACC3 is the same region utilised by DNA-binding classical zinc fingers to contact DNA. In addition to the multiple roles played by ZnFs, this domain is also known for its robustness and versatility. In Chapter 5, incomplete ZnF sequences were assessed for its ability to form functional zinc-binding domains. Remarkably, CCHX sequences (in the context of BKLF finger 3) were able to form discrete zinc-binding domains and also, mediate both protein-DNA and protein-protein interactions. This result not only illustrates the robust nature of ZnFs, it highlights the need for expanding ZnF sequence criteria when searching for functional zinc-binding modules. Together, the data presented here help further our understanding of zinc finger domains. Similar to the use of DNA-binding ZnFs in designer proteins, these data may start us on the path of designing novel protein-binding ZnFs.
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Garcia, Anderson. "Peptídeos derivados da proteína bacteriana YacG : síntese e estudos de estrutura-função /." Araraquara : [s.n.], 2010. http://hdl.handle.net/11449/87996.

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Resumo: YacG é uma pequena proteína (65 resíduos de aminoácidos) ligada ao zinco codificada pelo gene yacG de Escherichia coli. Seu papel fisiológico não está bem caracterizado, porém acredita-se que ela exerça ação inibitória sobre a atividade catalítica da DNA girase, enzima responsável por alterações no estado topológico do DNA bacteriano. Com base nas informações da estrutura primária desta proteína, uma série constituída de oito seqüências peptídicas foram projetadas e sintetizadas pela metodologia da fase sólida, objetivando-se avaliar e melhor entender o efeito da coordenação do íon zinco no seu mecanismo de ação. As sequências foram projetadas de maneira a resultar em uma substituição parcial ou integral dos resíduos de cisteína da sequência nativa da YacG, por resíduos de serina, além da variação da carga efetiva da molécula, por amidação ou acetilação das extremidades C e N terminais, respectivamente. Os peptídeos obtidos e purificados foram ensaiados quanto à estequiometria de coordenação empregando titulação com íon cobalto, bem como na capacidade inibitória frente à DNA girase, empregando eletroforese em gel de agarose. YacGAG4, inibiu a atividade de superenovelamento do DNA, catalisada pela girase, somente na ausência de íons zinco em concentrações inferiores a 120 μmol.L-1. Os demais peptídeos não apresentaram capacidade inibitória, tanto na presença quanto na ausência de zinco. Ensaios de susceptibilidade bacteriana, empregando algumas espécies de bactérias da família Enterobacteriaceae, confirmaram os resultados in vitro,com exceção das sequências YacGAG1-AC e YacGAG2-AC que mostraram inibição no crescimento bacteriano, sem porém resultarem em atividade in vitro. Com base nos resultados obtidos, é possível concluir que o domínio estrutural relacionado à coordenação do zinco, bem como a presença... (Resumo completo, clicar acesso eletrônico abaixo)<br>Abstract: YacG is a small protein (65 amino acid residues) bounded to zinc and encoded by the Escherichia coli yacG gene. Its physiological role is not well characterized, but it is believed that YacG is an inhibitor of the catalytic activity of DNA gyrase, an enzyme responsible for changes in the topological state of bacterial DNA. Based on information from the primary structure of this protein, a series of eight peptide sequences were designed and synthesized by solid phase methodology, aiming to evaluate and better understand the effect of zinc coordination of in their mechanism of action. The sequences were designed so as to result in a partial or full replacement of the cysteine residues of the native YacG sequence by serine residues and to change the effective charge of the molecule by amidation or acetylation of C and N terminal ends, respectively. The obtained peptides were purified and tested by titration with cobalt ion (coordination stoichiometry), as well as by inhibitory effect against the DNA gyrase, using agarose gel electrophoresis. YacGAG4 inhibited DNA supercoiling activity catalyzed by gyrase only in the zinc ions absence at concentrations below of 120 μmol.L-1. The other peptides showed no inhibitory effect in both the presence and absence of zinc. Bacterial susceptibility tests, using some species of bacteria of the Enterobacteriaceae, confirmed in vitro results, with the exception of the sequences YacGAG1-AC and YacGAG2-AC that showed inhibition of bacterial growth, but no in vitro activity. Based on these results, we conclude that the structural matters related to the coordination of zinc as well as the presence of this ion, showed no significant importance in the activity of DNA gyrase inhibition. In this case, the inhibition of activity recently proposed, should be linked to any other region of the protein molecule, structurally organized when the zinc ion is bound... (Complete abstract click electronic access below)<br>Orientador: Reinaldo Marchetto<br>Coorientador: Saulo Santesso Garrido<br>Banca: Clarice Queico Fujimura Leite<br>Banca: Vani Xavier de Oliveira Junior<br>Mestre
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Books on the topic "Zinc fingers"

1

Bibudhendra, Sarkar, and International Symposium on "Metals and Genetics" (1st : 1994 : Toronto, Ont.), eds. Genetic response to metals. M. Dekker, 1995.

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Liu, Jia, ed. Zinc Finger Proteins. Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8799-3.

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Iuchi, Shiro, and Natalie Kuldell, eds. Zinc Finger Proteins. Springer US, 2005. http://dx.doi.org/10.1007/b139055.

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Mackay, Joel P., and David J. Segal, eds. Engineered Zinc Finger Proteins. Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-753-2.

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Nagai, Ryōzō. The biology of Krüppel-like factors. Springer, 2009.

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1930-, Sluyser M., ed. Zinc-finger proteins in oncogenesis: DNA-binding and gene regulation. New York Academy of Sciences, 1993.

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Ferraz de Paiva, Raphael Enoque. Gold(I,III) Complexes Designed for Selective Targeting and Inhibition of Zinc Finger Proteins. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-030-00853-6.

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Pritchard, Jane. Analysis of drongo, a new Drosophila zinc finger gene expressed during oogenesis and neurogenesis. typescript, 1999.

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Hamburg, Universität, ed. Charakterisierung eines aus humanen T-Zellen isolierten Zink-Finger-Proteins (AT133). [s.n.], 1993.

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Perakakis, Nikolaos. The role of the zinc-finger transcription factor Krüppel-like factor 11 for gene regulation in pancreatic beta cells. s.n.], 2013.

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Book chapters on the topic "Zinc fingers"

1

Zeng, J., and J. H. R. Kägi. "Zinc Fingers and Metallothionein in Gene Expression." In Toxicology of Metals. Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79162-8_15.

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Rhodes, D., and A. Klug. "“Zinc Fingers”: A Novel Motif for Nucleic Acid Binding." In Nucleic Acids and Molecular Biology. Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-83384-7_9.

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De Franco, Simona, Mitchell R. O’Connell, and Marylène Vandevenne. "Engineering RNA-Binding Proteins by Modular Assembly of RanBP2-Type Zinc Fingers." In Methods in Molecular Biology. Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8799-3_5.

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Waryah, Charlene Babra, Colette Moses, Mahira Arooj, and Pilar Blancafort. "Zinc Fingers, TALEs, and CRISPR Systems: A Comparison of Tools for Epigenome Editing." In Methods in Molecular Biology. Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7774-1_2.

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De Guzman, Roberto N., Maria A. Martinez-Yamout, H. Jane Dyson, and Peter E. Wright. "Structure and Function of the CBP/p300 TAZ Domains." In Zinc Finger Proteins. Springer US, 2005. http://dx.doi.org/10.1007/0-387-27421-9_17.

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Van Roey, Patrick, Marlene Belfort, and Victoria Derbyshire. "Homing Endonuclease I-TevI: An Atypical Zinc Finger with a Novel Function." In Zinc Finger Proteins. Springer US, 2005. http://dx.doi.org/10.1007/0-387-27421-9_7.

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Shieh, Jia-Ching. "Bipartite Selection of Zinc Fingers by Phage Display for Any 9-bp DNA Target Site." In Methods in Molecular Biology. Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-753-2_3.

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Appella, E., J. G. Omichinski, G. M. Clore, A. M. Gronenborn, and K. Sakaguchi. "Zinc Fingers Involved in MHC Class I Gene Regulation: Use of Synthetic Peptides for Structural Analysis." In Methods in Protein Sequence Analysis. Birkhäuser Basel, 1991. http://dx.doi.org/10.1007/978-3-0348-5678-2_18.

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Biancalana, S., C. E. Dahl, H. T. Keutmann, D. Hudson, M. A. Marcus, and M. A. Weiss. "Biochemical and spectroscopic properties of DNA-binding zinc fingers: Application of Fmoc-mediated synthesis on PEG-polystyrene." In Peptides. Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2264-1_131.

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Wapnir, Raul A. "“Fingers”, “Knuckles”, “Hands”, “Fists”, “Signatures” and Other Structural Motifs in Proteins Involving Zinc and Other Essential Elements." In Protein Nutrition and Mineral Absorption. CRC Press, 2024. https://doi.org/10.1201/9781003574453-12.

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Conference papers on the topic "Zinc fingers"

1

"Protein-interacting C2H2-type zinc fingers: structural studies by NMR." In Биоинформатика регуляции и структуры геномов / системная биология. ИЦиГ СО РАН, 2024. http://dx.doi.org/10.18699/bgrs2024-3.1-45.

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Holden, Todd, G. Tremberger Jr., R. Sullivan, et al. "A Simple Di-Nucleotide Based DNA Analysis Applied to Phylogeny of Mammals using Zinc Fingers." In 2008 2nd International Conference on Bioinformatics and Biomedical Engineering. IEEE, 2008. http://dx.doi.org/10.1109/icbbe.2008.9.

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Liu, Zhihui, Wendy B. London, John Maris, and Carol J. Thiele. "Abstract 5015: Hcasz5, CASZ1 gene transcript variant 2 with 5 zinc fingers functions as a tumor suppressor in Neuroblastoma." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-5015.

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Vidovic, Karina. "Abstract 775: Mutant Wilms' tumor gene 1 devoid of zinc-fingers promotes proliferation of human hematopoietic progenitor cellsin vitro." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-775.

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Tremberger Jr., G., E. Cheung, R. Subramaniam, et al. "C2H2 Zinc Finger Nucleotide Fluctuation." In 2008 2nd International Conference on Bioinformatics and Biomedical Engineering. IEEE, 2008. http://dx.doi.org/10.1109/icbbe.2008.231.

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Sievers, Quinlan L., Georg Petzold, Richard D. Bunker, et al. "Abstract PL02-03: The zinc-finger degrome." In Abstracts: AACR-NCI-EORTC International Conference on Molecular Targets and Cancer Therapeutics; October 26-30, 2019; Boston, MA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1535-7163.targ-19-pl02-03.

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Tang, Mengxiang, Michael Waterman, and Shibu Yooseph. "Zinc finger gene clusters and tandem gene duplication." In the fifth annual international conference. ACM Press, 2001. http://dx.doi.org/10.1145/369133.369241.

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Novaković, Stefan, and Vladimir Risojević. "Learning Localization of Body and Finger Animation Skeleton Joints on Three-Dimensional Models of Human Bodies." In 2024 Zooming Innovation in Consumer Technologies Conference (ZINC). IEEE, 2024. http://dx.doi.org/10.1109/zinc61849.2024.10579426.

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Imtiaz, Jibran, Youngquan Shen, and Ronald Ellis. "Identifying Co-Factors That Drive TRA-1 Activator Function." In 27th Annual Rowan-Virtua Research Day. Rowan University Libraries, 2023. https://doi.org/10.31986/issn.2689-0690_rdw.stratford_research_day.124_2023.

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Gli proteins are involved in cell fate determination, proliferation, and patterning in many species and are major effectors of Hedgehog (Hh) signaling. There are three Gli proteins in humans, and mutations or errors in their regulation lead to a variety of developmental disorders or cancer. However, the mechanisms by which they interact with co-factors are poorly understood. We are analyzing co-factors of Gli proteins using TRA-1 in Caenorhabditis nematodes. The TRA-1 zinc fingers are structurally like those of other Gli proteins, and TRA-1 can be cleaved like other Gli proteins to form a repressor. However, its function has changed during evolution — in nematodes, TRA-1 controls sexual fates and plays a central role in self-fertility, which makes it easy to assay mutant phenotypes. Furthermore, worms lack classical Hedgehog signaling, so study of nematode TRA-1 should reveal other types of regulation. Our lab has shown that full-length TRA-1 can work as an activator and promote spermatogenesis, and that the mutation cbr-tra-1(v48) disrupts this process and prevents spermatogenesis. We suspect that regulation of TRA-1 activator plays a major role in the evolution of hermaphrodite spermatogenesis in nematodes. Because v48 was isolated in a classical EMS mutagenesis, we recently made other activator mutations to confirm that all of its phenotypes were due solely to the alteration of TRA-1. Since TRA-1 activator is likely to interact with a diverse set of co-factors, whose activities might help determine whether specific targets are activated or repressed, we identified sites in TRA-1 where an OLLAS tag does not inactivate the protein, and used anti-OLLAS antibodies to isolate TRA-1 complexes. We are now characterizing the products, and preparing to analyze them with mass spectrometry. While doing so, we will look for important modifications to TRA-1 itself, as well as the precise site of cleavage that forms the repressor. In addition, we hope to identify TRA-1 co-factors and learn how they regulate Gli activity. Finally, we will see if any of these co-factors has a novel role in species that produce self-fertile hermaphrodites
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Souza, Priscila M., Filomena M. Carvalho, Fernando N. Aguiar, Débora Gagliato, and Alfredo C. S. D. Barros. "ASSOCIATION BETWEEN GATA3 AND PATHOLOGIAL AND IMMUNOHISTOCHEMICAL PREDICTIVE AND PROGNOSTIC PARAMETERS IN EARLY BREAST CANCER." In Scientifc papers of XXIII Brazilian Breast Congress - 2021. Mastology, 2021. http://dx.doi.org/10.29289/259453942021v31s1046.

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Introduction: GATA3 gene, at 10p14, a member of the GATA family with two GATA-type zinc-fingers, encodes the transcription factors GATA - binding protein 3 (GATA3), critical for the luminal breast epithelium development and maintenance. The GATA3 protein is a linear one, with more than 400 aminoacids, that can be recognized by immunohistochemical analysis. Mutations of the GATA3 and loss of the expression of its related protein are implicated in breast cancer development and aggressiveness. As the most frequent transcription factor in luminal tumor cells, GATA3 became an important marker of mammary differentiation in neoplasias of unknown origin, better than mammaglobin and gross cystic disease fluid protein (GCDFP). Objectives: In this study, we aimed at assessing pathological and immunohistochemical variables and their association with GATA3 expression, adding bases for breast carcinogenesis comprehension and BC (Breast Cancer) precision therapy. Methods: GATA3 was analyzed by immunohistochemistry in whole histological sections of tumors from 105 female patients with histological diagnosis of invasive breast carcinoma and at clinical stages I, II and IIIA, who underwent primary surgical treatment (protocol approval number: 1,604,792). GATA3 nuclear expression was determined in percentage of tumor cells and categorized as preserved (positive expression in more than 95% of cells) or reduced (negative or expression in up to 95% of tumor cells). GATA3 expression was analyzed according to patient’s age, tumor and node pathological stage, histological type, histological and nuclear grade, lymphovascular invasion, estrogen receptor, progesterone receptor, androgen receptor, HER2 status, and Ki-67. Results: GATA3 expression was detected in 103/105 (98.1%) cases. Reduced expression was associated with higher histological and nuclear grade, negative hormonal receptors, HER2-positive and higher proliferative activity according to Ki-67 expression. Triple negative breast carcinomas (TNBC) and ER-negative/HER2-positive presented the highest frequency of GATA3 reduction (75%) compared to ER-positive/HER2-negative (4.1%) and ER-positive/HER2-positive (20%). Proliferative activity in TNBC tended to be higher among tumors with GATA3 reduced, irrespective of androgen receptor expression. In the group of ER-positive/ HER2-negative tumors only 3 cases presented GATA3 reduction, all of them with high proliferative activity. Conclusions: GATA3 expression is present in almost all cases of early breast cancer. Reduction in its expression is associated with adverse prognostic factors and higher proliferative activity in all subtypes, including ER-positive/HER2-negative tumors.
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Reports on the topic "Zinc fingers"

1

Hanas, Jay S. DEPSCOR/97-98 Mechanisms and Biomonitoring of Toxicant-Induced Changes in Zinc Finger Proteins. Defense Technical Information Center, 2002. http://dx.doi.org/10.21236/ada399974.

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Gmeiner, William H. Metal Occupancy of Zinc Finger Motifs as Determinants for Zn2+-Mediated Chemosensitization of Prostate Cancer Cells. Defense Technical Information Center, 2013. http://dx.doi.org/10.21236/ada596731.

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Rauscher III, Frank J. A Novel Strategy for Controlling the Metastic Phenotype: Targeting the SNAG Repression Domain in the SNAIL Zinc-Finger Protein. Defense Technical Information Center, 2003. http://dx.doi.org/10.21236/ada417783.

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Rauscher, III, and Frank J. A Novel Strategy for Controlling the Metastatic Phenotype: Targeting the SNAG Repression Domain in the SNAIL Zinc-Finger Protein. Defense Technical Information Center, 2007. http://dx.doi.org/10.21236/ada474599.

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Rauscher, Frank J., and III. A Novel Strategy for Controlling the Metastatic Phenotype: Targeting the SNAG Repression Domain in the SNAIL Zing-Finger Protein. Defense Technical Information Center, 2004. http://dx.doi.org/10.21236/ada427153.

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Paran, Ilan, and Allen Van Deynze. Regulation of pepper fruit color, chloroplasts development and their importance in fruit quality. United States Department of Agriculture, 2014. http://dx.doi.org/10.32747/2014.7598173.bard.

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Pepper exhibits large natural variation in chlorophyll content in the immature fruit. To dissect the genetic and molecular basis of this variation, we conducted QTL mapping for chlorophyll content in a cross between light and dark green-fruited parents, PI 152225 and 1154. Two major QTLs, pc1 and pc10, that control chlorophyll content by modulation of chloroplast compartment size in a fruit-specific manner were detected in chromosomes 1 and 10, respectively. The pepper homolog of GOLDEN2- LIKE transcription factor (CaGLK2) was found as underlying pc10, similar to its effect on tomato fruit chloroplast development. A candidate gene for pc1was found as controlling chlorophyll content in pepper by the modulation of chloroplast size and number. Fine mapping of pc1 aided by bulked DNA and RNA-seq analyses enabled the identification of a zinc finger transcription factor LOL1 (LSD-One-Like 1) as a candidate gene underlying pc1. LOL1 is a positive regulator of oxidative stress- induced cell death in Arabidopsis. However, over expression of the rice ortholog resulted in an increase of chlorophyll content. Interestingly, CaAPRR2 that is linked to the QTL and was found to affect immature pepper fruit color in a previous study, did not have a significant effect on chlorophyll content in the present study. Verification of the candidate's function was done by generating CRISPR/Cas9 knockout mutants of the orthologues tomato gene, while its knockout experiment in pepper by genome editing is under progress. Phenotypic similarity as a consequence of disrupting the transcription factor in both pepper and tomato indicated its functional conservation in controlling chlorophyll content in the Solanaceae. A limited sequence diversity study indicated that null mutations in CaLOL1 and its putative interactorCaMIP1 are present in C. chinensebut not in C. annuum. Combinations of mutations in CaLOL1, CaMIP1, CaGLK2 and CaAPRR2 are required for the creation of the extreme variation in chlorophyll content in Capsicum.
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Porat, Ron, Gregory T. McCollum, Amnon Lers, and Charles L. Guy. Identification and characterization of genes involved in the acquisition of chilling tolerance in citrus fruit. United States Department of Agriculture, 2007. http://dx.doi.org/10.32747/2007.7587727.bard.

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Citrus, like many other tropical and subtropical fruit are sensitive to chilling temperatures. However, application of a pre-storage temperature conditioning (CD) treatment at 16°C for 7 d or of a hot water brushing (HWB) treatment at 60°C for 20 sec remarkably enhances chilling tolerance and reduces the development of chilling injuries (CI) upon storage at 5°C. In the current research, we proposed to identify and characterize grapefruit genes that are induced by CD, and may contribute to the acquisition of fruit chilling tolerance, by two different molecular approaches: cDNA array analysis and PCR cDNA subtraction. In addition, following the recent development and commercialization of the new Affymetrix Citrus Genome Array, we further performed genome-wide transcript profiling analysis following exposure to CD and chilling treatments. To conduct the cDNA array analysis, we constructed cDNA libraries from the peel tissue of CD- and HWB-treated grapefruit, and performed an EST sequencing project including sequencing of 3,456 cDNAs from each library. Based on the obtained sequence information, we chose 70 stress-responsive and chilling-related genes and spotted them on nylon membranes. Following hybridization the constructed cDNA arrays with RNA probes from control and CD-treated fruit and detailed confirmations by RT-PCR analysis, we found that six genes: lipid-transfer protein, metallothionein-like protein, catalase, GTP-binding protein, Lea5, and stress-responsive zinc finger protein, showed higher transcript levels in flavedo of conditioned than in non-conditioned fruit stored at 5 ᵒC. The transcript levels of another four genes: galactinol synthase, ACC oxidase, temperature-induced lipocalin, and chilling-inducible oxygenase, increased only in control untreated fruit but not in chilling-tolerant CD-treated fruit. By PCR cDNA subtraction analysis we identified 17 new chilling-responsive and HWB- and CD-induced genes. Overall, characterization of the expression patterns of these genes as well as of 11 more stress-related genes by RNA gel blot hybridizations revealed that the HWB treatment activated mainly the expression of stress-related genes(HSP19-I, HSP19-II, dehydrin, universal stress protein, EIN2, 1,3;4-β-D-glucanase, and SOD), whereas the CD treatment activated mainly the expression of lipid modification enzymes, including fatty acid disaturase2 (FAD2) and lipid transfer protein (LTP). Genome wide transcriptional profiling analysis using the newly developed Affymetrix Citrus GeneChip® microarray (including 30,171 citrus probe sets) revealed the identification of three different chilling-related regulons: 1,345 probe sets were significantly affected by chilling in both control and CD-treated fruits (chilling-response regulon), 509 probe sets were unique to the CD-treated fruits (chilling tolerance regulon), and 417 probe sets were unique to the chilling-sensitive control fruits (chilling stress regulon). Overall, exposure to chilling led to expression governed arrest of general cellular metabolic activity, including concretive down-regulation of cell wall, pathogen defense, photosynthesis, respiration, and protein, nucleic acid and secondary metabolism. On the other hand, chilling enhanced various adaptation processes, such as changes in the expression levels of transcripts related to membranes, lipid, sterol and carbohydrate metabolism, stress stimuli, hormone biosynthesis, and modifications in DNA binding and transcription factors.
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