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Journal articles on the topic 'Zinc finger'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Li, Huiyu, Xiaomei Chen, Wei Xiong, Fang Liu, and Shiang Huang. "The Regulation of Zinc Finger Proteins by Mirnas Enriched in ALL-Microvesicles." Blood 120, no. 21 (2012): 1448. http://dx.doi.org/10.1182/blood.v120.21.1448.1448.

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Abstract Abstract 1448 Microvesicles (MVs) are submicrometric membrane fragments and they can “hijack” membrane components and engulf cytoplasmic contents from their cellular origin. MVs are enriched in various bioactive molecules of their parental cells, such as proteins, DNA, mRNA and miRNAs. Microvesicles (MVs) released by leukemia cells constitute an important part of the leukemia microenvironment. As a cell-to-cell communication tool, MVs transfer microRNA (miRNA) between cells. MVs miRNAs may also provide an insight in the role of miRNAs playing in the underlying of pathophysiologic proc

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2

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-contain

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3

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-contain

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4

Sievers, Quinlan L., Georg Petzold, Richard D. Bunker, et al. "Defining the human C2H2 zinc finger degrome targeted by thalidomide analogs through CRBN." Science 362, no. 6414 (2018): eaat0572. http://dx.doi.org/10.1126/science.aat0572.

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The small molecules thalidomide, lenalidomide, and pomalidomide induce the ubiquitination and proteasomal degradation of the transcription factors Ikaros (IKZF1) and Aiolos (IKZF3) by recruiting a Cys2-His2 (C2H2) zinc finger domain to Cereblon (CRBN), the substrate receptor of the CRL4CRBN E3 ubiquitin ligase. We screened the human C2H2 zinc finger proteome for degradation in the presence of thalidomide analogs, identifying 11 zinc finger degrons. Structural and functional characterization of the C2H2 zinc finger degrons demonstrates how diverse zinc finger domains bind the permissive drug-CR

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5

Witte, M. M., and R. C. Dickson. "The C6 zinc finger and adjacent amino acids determine DNA-binding specificity and affinity in the yeast activator proteins LAC9 and PPR1." Molecular and Cellular Biology 10, no. 10 (1990): 5128–37. http://dx.doi.org/10.1128/mcb.10.10.5128-5137.1990.

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LAC9 is a DNA-binding protein that regulates transcription of the lactose-galactose regulon in Kluyveromyces lactis. The DNA-binding domain is composed of a zinc finger and nearby amino acids (M. M. Witte and R. C. Dickson, Mol. Cell. Biol. 8:3726-3733, 1988). The single zinc finger appears to be structurally related to the zinc finger of many other fungal transcription activator proteins that contain positively charged residues and six conserved cysteines with the general form Cys-Xaa2-Cys-Xaa6-Cys-Xaa6-9-Cys-Xaa2-Cys-Xaa 6-Cys, where Xaan indicates a stretch of the indicated number of any am

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Witte, M. M., and R. C. Dickson. "The C6 zinc finger and adjacent amino acids determine DNA-binding specificity and affinity in the yeast activator proteins LAC9 and PPR1." Molecular and Cellular Biology 10, no. 10 (1990): 5128–37. http://dx.doi.org/10.1128/mcb.10.10.5128.

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LAC9 is a DNA-binding protein that regulates transcription of the lactose-galactose regulon in Kluyveromyces lactis. The DNA-binding domain is composed of a zinc finger and nearby amino acids (M. M. Witte and R. C. Dickson, Mol. Cell. Biol. 8:3726-3733, 1988). The single zinc finger appears to be structurally related to the zinc finger of many other fungal transcription activator proteins that contain positively charged residues and six conserved cysteines with the general form Cys-Xaa2-Cys-Xaa6-Cys-Xaa6-9-Cys-Xaa2-Cys-Xaa 6-Cys, where Xaan indicates a stretch of the indicated number of any am

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7

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 a

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8

Rollins, M. B., S. Del Rio, A. L. Galey, D. R. Setzer, and M. T. Andrews. "Role of TFIIIA zinc fingers in vivo: analysis of single-finger function in developing Xenopus embryos." Molecular and Cellular Biology 13, no. 8 (1993): 4776–83. http://dx.doi.org/10.1128/mcb.13.8.4776-4783.1993.

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The Xenopus 5S RNA gene-specific transcription factor IIIA (TFIIIA) has nine consecutive Cys2His2 zinc finger motifs. Studies were conducted in vivo to determine the contribution of each of the nine zinc fingers to the activity of TFIIIA in living cells. Nine separate TFIIIA mutants were expressed in Xenopus embryos following microinjection of their respective in vitro-derived mRNAs. Each mutant contained a single histidine-to-asparagine substitution in the third zinc ligand position of an individual zinc finger. These mutations result in structural disruption of the mutated finger with little

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9

Rollins, M. B., S. Del Rio, A. L. Galey, D. R. Setzer, and M. T. Andrews. "Role of TFIIIA zinc fingers in vivo: analysis of single-finger function in developing Xenopus embryos." Molecular and Cellular Biology 13, no. 8 (1993): 4776–83. http://dx.doi.org/10.1128/mcb.13.8.4776.

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The Xenopus 5S RNA gene-specific transcription factor IIIA (TFIIIA) has nine consecutive Cys2His2 zinc finger motifs. Studies were conducted in vivo to determine the contribution of each of the nine zinc fingers to the activity of TFIIIA in living cells. Nine separate TFIIIA mutants were expressed in Xenopus embryos following microinjection of their respective in vitro-derived mRNAs. Each mutant contained a single histidine-to-asparagine substitution in the third zinc ligand position of an individual zinc finger. These mutations result in structural disruption of the mutated finger with little

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10

Gebelein, Brian, and Raul Urrutia. "Sequence-Specific Transcriptional Repression by KS1, a Multiple-Zinc-Finger–Krüppel-Associated Box Protein." Molecular and Cellular Biology 21, no. 3 (2001): 928–39. http://dx.doi.org/10.1128/mcb.21.3.928-939.2001.

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ABSTRACT The vertebrate genome contains a large number of Krüppel-associated box–zinc finger genes that encode 10 or more C2-H2 zinc finger motifs. Members of this gene family have been proposed to function as transcription factors by binding DNA through their zinc finger region and repressing gene expression via the KRAB domain. To date, however, no Krüppel-associated box–zinc finger protein (KRAB-ZFP) and few proteins with 10 or more zinc finger motifs have been shown to bind DNA in a sequence-specific manner. Our laboratory has recently identified KS1, a member of the KRAB-ZFP family that

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11

Han, Guoliang, Ziqi Qiao, Yuxia Li, Chengfeng Wang, and Baoshan Wang. "The Roles of CCCH Zinc-Finger Proteins in Plant Abiotic Stress Tolerance." International Journal of Molecular Sciences 22, no. 15 (2021): 8327. http://dx.doi.org/10.3390/ijms22158327.

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Zinc-finger proteins, a superfamily of proteins with a typical structural domain that coordinates a zinc ion and binds nucleic acids, participate in the regulation of growth, development, and stress adaptation in plants. Most zinc fingers are C2H2-type or CCCC-type, named after the configuration of cysteine (C) and histidine (H); the less-common CCCH zinc-finger proteins are important in the regulation of plant stress responses. In this review, we introduce the domain structures, classification, and subcellular localization of CCCH zinc-finger proteins in plants and discuss their functions in

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12

Fu, Fengli, and Daniel F. Voytas. "Zinc Finger Database (ZiFDB) v2.0: a comprehensive database of C2H2 zinc fingers and engineered zinc finger arrays." Nucleic Acids Research 41, no. D1 (2012): D452—D455. http://dx.doi.org/10.1093/nar/gks1167.

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13

Fu, F., J. D. Sander, M. Maeder, et al. "Zinc Finger Database (ZiFDB): a repository for information on C2H2 zinc fingers and engineered zinc-finger arrays." Nucleic Acids Research 37, Database (2009): D279—D283. http://dx.doi.org/10.1093/nar/gkn606.

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14

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 aff

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15

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 aff

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16

Schulz, T. C., B. Hopwood, P. D. Rathjen, and J. R. Wells. "An unusual arrangement of 13 zinc fingers in the vertebrate gene Z13." Biochemical Journal 311, no. 1 (1995): 219–24. http://dx.doi.org/10.1042/bj3110219.

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The zinc finger is a protein domain that imparts specific nucleic acid-binding activity on a wide range of functionally important proteins. In this paper we report the molecular cloning and characterization of a novel murine zinc-finger gene, mZ13. Analysis of mZ13 cDNAs revealed that the gene expresses a 794-amino-acid protein encoded by a 2.7 kb transcript. The protein has an unusual arrangement of 13 zinc fingers into a ‘hand’ of 12 tandem fingers and a single isolated finger near the C-terminus. This structural organization is conserved with the probable chicken homologue, cZ13. mZ13 also

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17

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 use

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18

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 use

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19

Schjerven, Hilde, Seth Frietze, Jami McLaughlin, et al. "Role of Ikaros in hematopoiesis and tumor suppression: Selective functions of individual zinc fingers within the DNA-binding domain of Ikaros. (42.3)." Journal of Immunology 188, no. 1_Supplement (2012): 42.3. http://dx.doi.org/10.4049/jimmunol.188.supp.42.3.

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Abstract Ikaros, a C2H2 zinc finger transcription factor, is a critical regulator of hematopoiesis and tumor suppression in the lymphoid lineage. The C2H2 zinc finger is the most prevalent DNA-binding motif in mammals, with DNA-binding domains usually containing more tandem fingers than are needed for stable sequence-specific DNA recognition. To examine the reason for the frequent presence of multiple zinc fingers, and to investigate in greater depth the role of Ikaros in hematopoiesis and tumor suppression, we generated mice lacking finger 1 or finger 4 of the 4-finger DNA-binding domain of I

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20

Klug, Aaron. "The discovery of zinc fingers and their development for practical applications in gene regulation and genome manipulation." Quarterly Reviews of Biophysics 43, no. 1 (2010): 1–21. http://dx.doi.org/10.1017/s0033583510000089.

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AbstractA long-standing goal of molecular biologists has been to construct DNA-binding proteins for the control of gene expression. The classical Cys2His2 (C2H2) zinc finger design is ideally suited for such purposes. Discriminating between closely related DNA sequences both in vitro and in vivo, this naturally occurring design was adopted for engineering zinc finger proteins (ZFPs) to target genes specifically.Zinc fingers were discovered in 1985, arising from the interpretation of our biochemical studies on the interaction of the Xenopus protein transcription factor IIIA (TFIIIA) with 5S RNA

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21

Gianfrancesco, Olympia, Bethany Geary, Abigail L. Savage, Kimberley J. Billingsley, Vivien J. Bubb, and John P. Quinn. "The Role of SINE-VNTR-Alu (SVA) Retrotransposons in Shaping the Human Genome." International Journal of Molecular Sciences 20, no. 23 (2019): 5977. http://dx.doi.org/10.3390/ijms20235977.

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Retrotransposons can alter the regulation of genes both transcriptionally and post-transcriptionally, through mechanisms such as binding transcription factors and alternative splicing of transcripts. SINE-VNTR-Alu (SVA) retrotransposons are the most recently evolved class of retrotransposable elements, found solely in primates, including humans. SVAs are preferentially found at genic, high GC loci, and have been termed “mobile CpG islands”. We hypothesise that the ability of SVAs to mobilise, and their non-random distribution across the genome, may result in differential regulation of certain

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22

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

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23

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

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Gao, Xiang, Daniel J. Rowley, Xiaowu Gai, and Daniel F. Voytas. "Ty5 gag Mutations Increase Retrotransposition and Suggest a Role for Hydrogen Bonding in the Function of the Nucleocapsid Zinc Finger." Journal of Virology 76, no. 7 (2002): 3240–47. http://dx.doi.org/10.1128/jvi.76.7.3240-3247.2002.

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ABSTRACT The Ty5 retrotransposon of Saccharomyces paradoxus transposes in Saccharomyces cerevisiae at frequencies 1,000-fold lower than do the native Ty1 elements. The low transposition activity of Ty5 could be due to differences in cellular environments between these yeast species or to naturally occurring mutations in Ty5. By screening of a Ty5 mutant library, two single mutants (D252N and Y68C) were each found to increase transposition approximately sixfold. When combined, transposition increased 36-fold, implying that the two mutations act independently. Neither mutation affected Ty5 prote

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Smith, Alexander E. F., Farzin Farzaneh, and Kevin G. Ford. "Single zinc-finger extension: enhancing transcriptional activity and specificity of three-zinc-finger proteins." Biological Chemistry 386, no. 2 (2005): 95–99. http://dx.doi.org/10.1515/bc.2005.012.

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AbstractIn order to demonstrate that an existing zinc-finger protein can be simply modified to enhance DNA binding and sequence discrimination in both episomal and chromatin contexts using existing zinc-finger DNA recognition code data, and without recourse to phage display and selection strategies, we have examined the consequences of a single zinc-finger extension to a synthetic three-zinc-finger VP16 fusion protein, on transcriptional activation from model target promoters harbouring the zinc-finger binding sequences. We report a nearly 10-fold enhanced transcriptional activation by the fou

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26

Kanakoglou, Dimitrios S., Andromachi Pampalou, Lina S. Malakou, et al. "Central Role of C2H2-Type Zinc Finger-Containing Genes in Pediatric Brain Tumors." DNA 2, no. 1 (2022): 1–21. http://dx.doi.org/10.3390/dna2010001.

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Zinc fingers consist of one of the most abundant motifs in transcription factors and DNA-binding proteins. Recent studies provide evidence on the pathological implication of zinc finger proteins in various neurodevelopmental disorders and malignancies but their role in pediatric brain tumors is largely unexplored. To this end, we investigated the differential expression of zinc finger-containing genes along with relevant biological processes and pathways among four main brain tumor categories (pilocytic astrocytomas, ependymomas, medulloblastomas and glioblastomas). By employing an extended bi

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27

Shastry, B. S. "Transcription factor IIIA (TFIIIA) in the second decade." Journal of Cell Science 109, no. 3 (1996): 535–39. http://dx.doi.org/10.1242/jcs.109.3.535.

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Transcription factor IIIA is a very extensively studied eukaryotic gene specific factor. It is a special member of the zinc finger family of nucleic acid binding proteins with multiple functions. Its N-terminal polypeptide (280 amino acid residue containing peptide; finger containing region) carries out sequence specific DNA and RNA binding and the C-terminal peptide (65 amino acid residue containing peptide; non-finger region) is involved in the transactivation process possibly by interacting with other general factors. It is a unique factor in the sense that it binds to two structurally diff

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Zhang, XiaoHong, YuJi Miao, XiaoDan Hu, Rui Min, PeiDang Liu, and HaiQian Zhang. "Gamma Radiation-Induced Damage in the Zinc Finger of the Transcription Factor IIIA." Bioinorganic Chemistry and Applications 2016 (2016): 1–7. http://dx.doi.org/10.1155/2016/1642064.

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A zinc finger motif is an element of proteins that can specifically recognize and bind to DNA. Because they contain multiple cysteine residues, zinc finger motifs possess redox properties. Ionizing radiation generates a variety of free radicals in organisms. Zinc finger motifs, therefore, may be a target of ionizing radiation. The effect of gamma radiation on the zinc finger motifs in transcription factor IIIA (TFIIIA), a zinc finger protein, was investigated. TFIIIA was exposed to different gamma doses from 60Co sources. The dose rates were 0.20 Gy/min and 800 Gy/h, respectively. The binding

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29

de Souza, Natalie. "Zinc-finger nucleases." Nature Methods 8, no. 1 (2010): 43. http://dx.doi.org/10.1038/nmeth.f.328.

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Schmiedeskamp, Mia, and Rachel E. Klevit. "Zinc finger diversity." Current Opinion in Structural Biology 4, no. 1 (1994): 28–35. http://dx.doi.org/10.1016/s0959-440x(94)90056-6.

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Kaptein, Robert. "Zinc-finger structures." Current Biology 2, no. 3 (1992): 126. http://dx.doi.org/10.1016/0960-9822(92)90247-8.

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Kaptein, Robert. "Zinc-finger structures." Current Opinion in Structural Biology 2, no. 1 (1992): 109–15. http://dx.doi.org/10.1016/0959-440x(92)90185-a.

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Berg, Jeremy M. "Zinc-finger proteins." Current Opinion in Structural Biology 3, no. 1 (1993): 11–16. http://dx.doi.org/10.1016/0959-440x(93)90195-q.

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Sander, J. D., M. L. Maeder, D. Reyon, D. F. Voytas, J. K. Joung, and D. Dobbs. "ZiFiT (Zinc Finger Targeter): an updated zinc finger engineering tool." Nucleic Acids Research 38, Web Server (2010): W462—W468. http://dx.doi.org/10.1093/nar/gkq319.

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35

Belczyk-Ciesielska, Agnieszka, Brigitta Csipak, Bálint Hajdu, et al. "Nickel(ii)-promoted specific hydrolysis of zinc finger proteins." Metallomics 10, no. 8 (2018): 1089–98. http://dx.doi.org/10.1039/c8mt00098k.

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The (S/T)XH sequence in Cys<sub>2</sub>His<sub>2</sub>zinc fingers can be hydrolytically cleaved by Ni(ii) ions. This reaction can be applied for purification, inhibition or activation of designed zinc finger fusion proteins.

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Guo, Jianhui, Tiyun Wu, Jada Anderson, et al. "Zinc Finger Structures in the Human Immunodeficiency Virus Type 1 Nucleocapsid Protein Facilitate Efficient Minus- and Plus-Strand Transfer." Journal of Virology 74, no. 19 (2000): 8980–88. http://dx.doi.org/10.1128/jvi.74.19.8980-8988.2000.

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ABSTRACT The nucleocapsid protein (NC) of human immunodeficiency virus type 1 (HIV-1) has two zinc fingers, each containing the invariant metal ion binding residues CCHC. Recent reports indicate that mutations in the CCHC motifs are deleterious for reverse transcription in vivo. To identify reverse transcriptase (RT) reactions affected by such changes, we have probed zinc finger functions in NC-dependent RT-catalyzed HIV-1 minus- and plus-strand transfer model systems. Our approach was to examine the activities of wild-type NC and a mutant in which all six cysteine residues were replaced by se

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Buck-Koehntop, Bethany A., Robyn L. Stanfield, Damian C. Ekiert, et al. "Molecular basis for recognition of methylated and specific DNA sequences by the zinc finger protein Kaiso." Proceedings of the National Academy of Sciences 109, no. 38 (2012): 15229–34. http://dx.doi.org/10.1073/pnas.1213726109.

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Methylation of CpG dinucleotides in DNA is a common epigenetic modification in eukaryotes that plays a central role in maintenance of genome stability, gene silencing, genomic imprinting, development, and disease. Kaiso, a bifunctional Cys2His2 zinc finger protein implicated in tumor-cell proliferation, binds to both methylated CpG (mCpG) sites and a specific nonmethylated DNA motif (TCCTGCNA) and represses transcription by recruiting chromatin remodeling corepression machinery to target genes. Here we report structures of the Kaiso zinc finger DNA-binding domain in complex with its nonmethyla

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Kaiming, Cao, Yaping Sheng, Shihui Zheng, Siming Yuan, Guangming Huang, and Yangzhong Liu. "Arsenic trioxide preferentially binds to the ring finger protein PML: understanding target selection of the drug." Metallomics 10, no. 11 (2018): 1564–69. http://dx.doi.org/10.1039/c8mt00202a.

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Huan, Chen, Cai Xiaoxu, and Ren Xifang. "Zinc Finger Protein 521, Negatively Regulated by MicroRNA-204-5p, Promotes Proliferation, Motility and Invasion of Gastric Cancer Cells." Technology in Cancer Research & Treatment 18 (January 1, 2019): 153303381987478. http://dx.doi.org/10.1177/1533033819874783.

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Objective: This study aims to investigate the expression, role, and detailed mechanism of microRNA-204-5p and zinc finger protein 521 in gastric cancer. Methods: Immunohistochemistry was adopted to detect the expressions of zinc finger protein 521 in 82 cases of gastric cancer tissues. Western blot was used to detect the expressions of zinc finger protein 521 in gastric cancer cells and adjacent cells. Moreover, the correlation between zinc finger protein 521 and the prognosis of patients were also evaluated. Cell Counting Kit 8 assay and colony formation assay were performed to figure out the

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Guo, Xuemin, John-William N. Carroll, Margaret R. MacDonald, Stephen P. Goff, and Guangxia Gao. "The Zinc Finger Antiviral Protein Directly Binds to Specific Viral mRNAs through the CCCH Zinc Finger Motifs." Journal of Virology 78, no. 23 (2004): 12781–87. http://dx.doi.org/10.1128/jvi.78.23.12781-12787.2004.

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ABSTRACT The zinc finger antiviral protein (ZAP) is a recently isolated host antiviral factor. It specifically inhibits the replication of Moloney murine leukemia virus (MLV) and Sindbis virus (SIN) by preventing the accumulation of viral RNA in the cytoplasm. For this report, we mapped the viral sequences that are sensitive to ZAP inhibition. The viral sequences were cloned into a luciferase reporter and analyzed for the ability to mediate ZAP-dependent destabilization of the reporter. The sensitive sequence in MLV was mapped to the 3′ long terminal repeat; the sensitive sequences in SIN were

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Blobel, G. A., M. C. Simon, and S. H. Orkin. "Rescue of GATA-1-deficient embryonic stem cells by heterologous GATA-binding proteins." Molecular and Cellular Biology 15, no. 2 (1995): 626–33. http://dx.doi.org/10.1128/mcb.15.2.626.

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Totipotent murine embryonic stem (ES) cells can be differentiated in vitro to form embryoid bodies (EBs) containing hematopoietic cells of multiple lineages, including erythroid cells. In vitro erythroid development parallels that which is observed in vivo. ES cells in which the gene for the erythroid transcription factor GATA-1 has been disrupted fail to produce mature erythroid cells either in vivo or in vitro. With the EB in vitro differentiation assay, constructs expressing heterologous GATA-binding proteins were tested for their abilities to correct the developmental defect of GATA-1-defi

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Witzgall, R., E. O'Leary, R. Gessner, A. J. Ouellette, and J. V. Bonventre. "Kid-1, a putative renal transcription factor: regulation during ontogeny and in response to ischemia and toxic injury." Molecular and Cellular Biology 13, no. 3 (1993): 1933–42. http://dx.doi.org/10.1128/mcb.13.3.1933-1942.1993.

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We have identified a new putative transcription factor from the rat kidney, termed Kid-1 (for kidney, ischemia and developmentally regulated gene 1). Kid-1 belongs to the C2H2 class of zinc finger genes. Its mRNA accumulates with age in postnatal renal development and is detected predominantly in the kidney. Kid-1 mRNA levels decline after renal injury secondary to ischemia or folic acid administration, two insults which result in epithelial cell dedifferentiation, followed by regenerative hyperplasia and differentiation. The low expression of Kid-1 early in postnatal development, and when ren

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Witzgall, R., E. O'Leary, R. Gessner, A. J. Ouellette, and J. V. Bonventre. "Kid-1, a putative renal transcription factor: regulation during ontogeny and in response to ischemia and toxic injury." Molecular and Cellular Biology 13, no. 3 (1993): 1933–42. http://dx.doi.org/10.1128/mcb.13.3.1933.

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We have identified a new putative transcription factor from the rat kidney, termed Kid-1 (for kidney, ischemia and developmentally regulated gene 1). Kid-1 belongs to the C2H2 class of zinc finger genes. Its mRNA accumulates with age in postnatal renal development and is detected predominantly in the kidney. Kid-1 mRNA levels decline after renal injury secondary to ischemia or folic acid administration, two insults which result in epithelial cell dedifferentiation, followed by regenerative hyperplasia and differentiation. The low expression of Kid-1 early in postnatal development, and when ren

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Chavrier, P., P. Lemaire, O. Revelant, R. Bravo, and P. Charnay. "Characterization of a mouse multigene family that encodes zinc finger structures." Molecular and Cellular Biology 8, no. 3 (1988): 1319–26. http://dx.doi.org/10.1128/mcb.8.3.1319-1326.1988.

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The Drosophila segmentation gene Krüppel encodes multiple tandemly repeated units predicted to form DNA-binding zinc fingers. We have isolated 23 bacteriophages, containing nonoverlapping inserts from a mouse genomic DNA library, on the basis of cross-hybridization under nonstringent conditions to a probe corresponding to the Krüppel finger region. Nucleotide sequence analysis of six phage DNAs indicated that they all contained regions with similarity to Krüppel and potentially encoded zinc finger domains. Within these regions, the level of similarity to Krüppel was particularly high between s

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Chavrier, P., P. Lemaire, O. Revelant, R. Bravo, and P. Charnay. "Characterization of a mouse multigene family that encodes zinc finger structures." Molecular and Cellular Biology 8, no. 3 (1988): 1319–26. http://dx.doi.org/10.1128/mcb.8.3.1319.

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The Drosophila segmentation gene Krüppel encodes multiple tandemly repeated units predicted to form DNA-binding zinc fingers. We have isolated 23 bacteriophages, containing nonoverlapping inserts from a mouse genomic DNA library, on the basis of cross-hybridization under nonstringent conditions to a probe corresponding to the Krüppel finger region. Nucleotide sequence analysis of six phage DNAs indicated that they all contained regions with similarity to Krüppel and potentially encoded zinc finger domains. Within these regions, the level of similarity to Krüppel was particularly high between s

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Luo, Z., B. Diaz, M. S. Marshall, and J. Avruch. "An intact Raf zinc finger is required for optimal binding to processed Ras and for ras-dependent Raf activation in situ." Molecular and Cellular Biology 17, no. 1 (1997): 46–53. http://dx.doi.org/10.1128/mcb.17.1.46.

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The function of the c-Raf-1 zinc finger domain in the activation of the Raf kinase was examined by the creation of variant zinc finger structures. Mutation of Raf Cys 165 and Cys 168 to Ser strongly inhibits the Ras-dependent activation of c-Raf-1 by epidermal growth factor (EGF). Deletion of the Raf zinc finger and replacement with a homologous zinc finger from protein kinase C gamma (PKC gamma) (to give gamma/Raf) also abrogates EGF-induced activation but enables a vigorous phorbol myristate acetate (PMA)-induced activation. PMA activation of gamma/Raf does not require endogenous Ras or PKCs

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Galdieri, Luciano, Mitchell Grinwald, Zibi Gugala, Edward Oates, and Milan Chheda. "STEM-13. FUNCTIONAL CHARACTERIZATION OF THE ZFHX4-CHD4 INTERACTION IN GLIOBLASTOMA CANCER STEM CELLS." Neuro-Oncology 22, Supplement_2 (2020): ii199. http://dx.doi.org/10.1093/neuonc/noaa215.830.

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Abstract Glioblastoma stem cells (GSCs) they may be one reason for inevitable recurrence of GBM. We previously discovered that Zinc Finger Homeobox 4 (ZFHX4), a 450kD transcription factor, is required to maintain the GSC state. ZFHX4 interacts with CHD4, a core member of the nucleosome remodeling and deacetylase (NuRD) complex, which activates or represses gene expression via two distinct functions - histone deacetylation and ATP-dependent chromatin remodeling. CHD4 suppression phenocopies ZFHX4 suppression. The precise nature and function of the ZFHX4 interaction with CHD4 is not understood.

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Prunuske, Amy J., Jin Liu, Suzanne Elgort, Jomon Joseph, Mary Dasso, and Katharine S. Ullman. "Nuclear Envelope Breakdown Is Coordinated by Both Nup358/RanBP2 and Nup153, Two Nucleoporins with Zinc Finger Modules." Molecular Biology of the Cell 17, no. 2 (2006): 760–69. http://dx.doi.org/10.1091/mbc.e05-06-0485.

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When higher eukaryotic cells transition into mitosis, the nuclear envelope, nuclear pore complexes, and nuclear lamina are coordinately disassembled. The COPI coatomer complex, which plays a major role in membrane remodeling at the Golgi, has been implicated in the process of nuclear envelope breakdown and requires interactions at the nuclear pore complex for recruitment to this new site of action at mitosis. Nup153, a resident of the nuclear pore basket, was found to be involved in COPI recruitment, but the molecular nature of the interface between COPI and the nuclear pore has not been fully

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Estruch, F., and M. Carlson. "Two homologous zinc finger genes identified by multicopy suppression in a SNF1 protein kinase mutant of Saccharomyces cerevisiae." Molecular and Cellular Biology 13, no. 7 (1993): 3872–81. http://dx.doi.org/10.1128/mcb.13.7.3872-3881.1993.

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The MSN2 gene was selected as a multicopy suppressor in a temperature-sensitive SNF1 protein kinase mutant of Saccharomyces cerevisiae. MSN2 encodes a Cys2His2 zinc finger protein related to the yeast MIG1 repressor and to mammalian early growth response and Wilms' tumor zinc finger proteins. Deletion of MSN2 caused no phenotype. A second similar zinc finger gene, MSN4, was isolated, and deletion of both genes caused phenotypic defects related to carbon utilization. Overexpression of the zinc finger regions was deleterious to growth. LexA-MSN2 and LexA-MSN4 fusion proteins functioned as strong

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Estruch, F., and M. Carlson. "Two homologous zinc finger genes identified by multicopy suppression in a SNF1 protein kinase mutant of Saccharomyces cerevisiae." Molecular and Cellular Biology 13, no. 7 (1993): 3872–81. http://dx.doi.org/10.1128/mcb.13.7.3872.

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The MSN2 gene was selected as a multicopy suppressor in a temperature-sensitive SNF1 protein kinase mutant of Saccharomyces cerevisiae. MSN2 encodes a Cys2His2 zinc finger protein related to the yeast MIG1 repressor and to mammalian early growth response and Wilms' tumor zinc finger proteins. Deletion of MSN2 caused no phenotype. A second similar zinc finger gene, MSN4, was isolated, and deletion of both genes caused phenotypic defects related to carbon utilization. Overexpression of the zinc finger regions was deleterious to growth. LexA-MSN2 and LexA-MSN4 fusion proteins functioned as strong

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