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Journal articles on the topic 'Transcription factor IIIA-interacting protein'

Author: Grafiati

Published: 4 June 2025

Last updated: 1 August 2025

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1

Moreland, R. J., M. E. Dresser, J. S. Rodgers, et al. "Identification of a transcription factor IIIA-interacting protein." Nucleic Acids Research 28, no. 9 (2000): 1986–93. http://dx.doi.org/10.1093/nar/28.9.1986.

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2

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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3

Wyszko, E., M. Radłowski, S. Bartkowiak, and M. Z. Barciszewska. "Maize TF IIIA--the first transcription factor IIIA from monocotyledons. Purification and properties." Acta Biochimica Polonica 44, no. 3 (1997): 579–89. http://dx.doi.org/10.18388/abp.1997_4406.

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Purification and properties of transcription factor IIIA (TF IIIA) from maize pollen (Zea mays L.) are presented for the first time. The purified protein has a molecular mass of about 35 kDa and exhibits binding affinity toward both 5S rRNA and 5S rRNA gene. It also facilitates transcription of the 5S rRNA gene in a HeLa cell extract.

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4

Hall, R. K., and W. L. Taylor. "Transcription factor IIIA gene expression in Xenopus oocytes utilizes a transcription factor similar to the major late transcription factor." Molecular and Cellular Biology 9, no. 11 (1989): 5003–11. http://dx.doi.org/10.1128/mcb.9.11.5003-5011.1989.

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Xenopus transcription factor IIIA (TFIIIA) gene expression is stringently regulated during development. The steady-state level of TFIIIA mRNA in a somatic cell is approximately 10(6) times less than in an immature oocyte. We have undertaken studies designed to identify differences in how the TFIIIA gene is transcribed in oocytes and somatic cells. In this regard, we have localized an upstream transcriptional control element in the TFIIIA promoter that stimulates transcription from the TFIIIA promoter approximately threefold in microinjected oocytes. The upstream element, in cis. does not stimu

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5

Hall, R. K., and W. L. Taylor. "Transcription factor IIIA gene expression in Xenopus oocytes utilizes a transcription factor similar to the major late transcription factor." Molecular and Cellular Biology 9, no. 11 (1989): 5003–11. http://dx.doi.org/10.1128/mcb.9.11.5003.

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Xenopus transcription factor IIIA (TFIIIA) gene expression is stringently regulated during development. The steady-state level of TFIIIA mRNA in a somatic cell is approximately 10(6) times less than in an immature oocyte. We have undertaken studies designed to identify differences in how the TFIIIA gene is transcribed in oocytes and somatic cells. In this regard, we have localized an upstream transcriptional control element in the TFIIIA promoter that stimulates transcription from the TFIIIA promoter approximately threefold in microinjected oocytes. The upstream element, in cis. does not stimu

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6

CHEN, Feifei, Kenji OGAWA, Raman P. NAGARAJAN, Meiyu ZHANG, Chenzhong KUANG, and Yan CHEN. "Regulation of TG-interacting factor by transforming growth factor-beta." Biochemical Journal 371, no. 2 (2003): 257–63. http://dx.doi.org/10.1042/bj20030095.

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TG-interacting factor (TGIF) is a transcriptional co-repressor that directly associates with Smad (Sma- and Mad-related protein) proteins and inhibits Smad-mediated transcriptional activation. By using Affymetrix (Santa Clara, CA, U.S.A.) oligonucleotide microarray analysis, we found that TGIF mRNA level was elevated by transforming-growth-factor-β (TGF-β) treatment in a human T-cell line, HuT78. Subsequent reverse-transcription PCR assays indicated that TGF-β1 and activin were able to induce a rapid and transient increase in the level of TGIF in both HuT78 and HepG2 hepatoma cells. To analyse

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7

Kołodziej, Marta, Panagiotis Tsapras, Alexander D. Cameron, and Ioannis P. Nezis. "Transcription Factor Deformed Wings Is an Atg8a-Interacting Protein That Regulates Autophagy." Cells 13, no. 22 (2024): 1897. http://dx.doi.org/10.3390/cells13221897.

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LC3 (microtubule-associated protein 1 light chain 3, called Atg8 in yeast and Drosophila) is one of the most well-studied autophagy-related proteins. LC3 controls the selectivity of autophagic degradation by interacting with LIR (LC3-interacting region) motifs also known as AIM (Atg8-interacting motifs) on selective autophagy receptors that carry cargo for degradation. Although the function of Atg8 family proteins is primarily cytoplasmic, they are also enriched in the nucleus. Despite the accumulating evidence indicating the presence of Atg8 proteins in the nucleus, the mechanisms by which th

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8

Kitagawa, Takao, Daiki Kobayashi, Byron Baron, et al. "AT-hook DNA-binding motif-containing protein one knockdown downregulates EWS-FLI1 transcriptional activity in Ewing’s sarcoma cells." PLOS ONE 17, no. 10 (2022): e0269077. http://dx.doi.org/10.1371/journal.pone.0269077.

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Ewing’s sarcoma is the second most common bone malignancy in children or young adults and is caused by an oncogenic transcription factor by a chromosomal translocation between the EWSR1 gene and the ETS transcription factor family. However, the transcriptional mechanism of EWS-ETS fusion proteins is still unclear. To identify the transcriptional complexes of EWS-ETS fusion transcription factors, we applied a proximal labeling system called BioID in Ewing’s sarcoma cells. We identified AHDC1 as a proximal protein of EWS-ETS fusion proteins. AHDC1 knockdown showed a reduced cell growth and trans

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9

Palvimo, J. J. "PIAS proteins as regulators of small ubiquitin-related modifier (SUMO) modifications and transcription." Biochemical Society Transactions 35, no. 6 (2007): 1405–8. http://dx.doi.org/10.1042/bst0351405.

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Transcriptional activity of signal-dependent transcription factors, including nuclear receptors, relies on interacting co-regulator proteins, many of which possess protein-modifying activity. SUMOs (small ubiquitin-related modifiers) and their conjugation pathway components act as co-regulator proteins for numerous transcription factors that also are often targets for SUMO modification. PIAS [protein inhibitor of activated STAT (signal transducer and activator of transcription)] proteins promote SUMOylation in a manner that resembles the action of RING-type ubiquitin E3 ligases. PIAS proteins

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10

Shimojo, Masahito, and Louis B. Hersh. "REST/NRSF-Interacting LIM Domain Protein, a Putative Nuclear Translocation Receptor." Molecular and Cellular Biology 23, no. 24 (2003): 9025–31. http://dx.doi.org/10.1128/mcb.23.24.9025-9031.2003.

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ABSTRACT The transcriptional repressor REST/NRSF (RE-1 silencing transcription factor/neuron-restrictive silencer factor) and the transcriptional regulator REST4 share an N-terminal zinc finger domain structure involved in nuclear targeting. Using this domain as bait in a yeast two-hybrid screen, a novel protein that contains three LIM domains, putative nuclear localization sequences, protein kinase A phosphorylation sites, and a CAAX prenylation motif was isolated. This protein, which is localized around the nucleus, is involved in determining the nuclear localization of REST4 and REST/NRSF.

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11

Schiff, L. A., M. L. Nibert, M. S. Co, E. G. Brown, and B. N. Fields. "Distinct binding sites for zinc and double-stranded RNA in the reovirus outer capsid protein sigma 3." Molecular and Cellular Biology 8, no. 1 (1988): 273–83. http://dx.doi.org/10.1128/mcb.8.1.273-283.1988.

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By atomic absorption analysis, we determined that the reovirus outer capsid protein sigma 3, which binds double-stranded RNA (dsRNA), is a zinc metalloprotein. Using Northwestern blots and a novel zinc blotting technique, we localized the zinc- and dsRNA-binding activities of sigma 3 to distinct V8 protease-generated fragments. Zinc-binding activity was contained within an amino-terminal fragment that contained a transcription factor IIIA-like zinc-binding sequence, and dsRNA-binding activity was associated with a carboxy-terminal fragment. By these techniques, new zinc- and dsRNA-binding acti

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12

Schiff, L. A., M. L. Nibert, M. S. Co, E. G. Brown, and B. N. Fields. "Distinct binding sites for zinc and double-stranded RNA in the reovirus outer capsid protein sigma 3." Molecular and Cellular Biology 8, no. 1 (1988): 273–83. http://dx.doi.org/10.1128/mcb.8.1.273.

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By atomic absorption analysis, we determined that the reovirus outer capsid protein sigma 3, which binds double-stranded RNA (dsRNA), is a zinc metalloprotein. Using Northwestern blots and a novel zinc blotting technique, we localized the zinc- and dsRNA-binding activities of sigma 3 to distinct V8 protease-generated fragments. Zinc-binding activity was contained within an amino-terminal fragment that contained a transcription factor IIIA-like zinc-binding sequence, and dsRNA-binding activity was associated with a carboxy-terminal fragment. By these techniques, new zinc- and dsRNA-binding acti

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13

Bazett-Jones, D. P., and M. L. Brown. "Electron microscopy reveals that transcription factor TFIIIA bends 5S DNA." Molecular and Cellular Biology 9, no. 1 (1989): 336–41. http://dx.doi.org/10.1128/mcb.9.1.336-341.1989.

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We have used a high-resolution analytical electron microscopic technique, electron spectroscopic imaging, to study the in vitro interaction between the transcription factor IIIA (TFIIIA) and 5S ribosomal gene DNA. The images and analytical measurements support our proposal that the helix axis is bent by the protein into a hairpin-shaped configuration.

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14

Bazett-Jones, D. P., and M. L. Brown. "Electron microscopy reveals that transcription factor TFIIIA bends 5S DNA." Molecular and Cellular Biology 9, no. 1 (1989): 336–41. http://dx.doi.org/10.1128/mcb.9.1.336.

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We have used a high-resolution analytical electron microscopic technique, electron spectroscopic imaging, to study the in vitro interaction between the transcription factor IIIA (TFIIIA) and 5S ribosomal gene DNA. The images and analytical measurements support our proposal that the helix axis is bent by the protein into a hairpin-shaped configuration.

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15

Nagulapalli, S., J. M. Pongubala, and M. L. Atchison. "Multiple proteins physically interact with PU.1. Transcriptional synergy with NF-IL6 beta (C/EBP delta, CRP3)." Journal of Immunology 155, no. 9 (1995): 4330–38. http://dx.doi.org/10.4049/jimmunol.155.9.4330.

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Abstract PU.1 is a transcription factor that belongs to the ets family of DNA binding proteins. In this study, we show by Far Western blot analyses that multiple nuclear proteins are capable of physically interacting with PU.1. Using radiolabeled PU.1 protein as a probe, we screened a B cell cDNA expression library and isolated a number of clones encoding PU.1 interacting proteins. Three of these clones encode DNA binding proteins (NF-IL6 beta, HMG I/Y, and SSRP), one clone encodes a chaperone protein, and another clone encodes a multifunctional phosphatase. We have characterized the physical

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16

WESTMARK, Cara J., Romi GHOSE, and Paul W. HUBER. "Phosphorylation of Xenopus transcription factor IIIA by an oocyte protein kinase CK2." Biochemical Journal 362, no. 2 (2002): 375. http://dx.doi.org/10.1042/0264-6021:3620375.

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17

WESTMARK, Cara J., Romi GHOSE, and Paul W. HUBER. "Phosphorylation of Xenopus transcription factor IIIA by an oocyte protein kinase CK2." Biochemical Journal 362, no. 2 (2002): 375–82. http://dx.doi.org/10.1042/bj3620375.

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Transcription factor IIIA (TFIIIA), isolated from the cytoplasmic 7S ribonucleoprotein complex of Xenopus oocytes, is phosphorylated when incubated with [γ-32P]ATP. This modification is due to a trace kinase activity that remains associated with the factor through several steps of purification. The kinase can use either ATP or GTP, and will phosphorylate casein and phosvitin to the exclusion of TFIIIA. The kinase is reactive with a ten-amino-acid peptide that is a specific substrate for protein kinase CK2 (CK2; formerly casein kinase II). In addition, inhibition of phosphorylation by heparin a

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18

Miller, J., A. D. McLachlan, and A. Klug. "Repetitive zinc-binding domains in the protein transcription factor IIIA fromXenopus oocytes." Journal of Trace Elements in Experimental Medicine 14, no. 2 (2001): 157–69. http://dx.doi.org/10.1002/jtra.1022.

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19

Abraham, Saji, Raghavendra Paknikar, Samina Bhumbra, et al. "Epigenetic regulation of arginine vasopressin receptor 2 expression by PAX2 and Pax transcription interacting protein." American Journal of Physiology-Renal Physiology 320, no. 3 (2021): F404—F417. http://dx.doi.org/10.1152/ajprenal.00371.2020.

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The transcription factor PAX2 plays an indispensable role in kidney development. In the adult kidney, we identified the first described protein this protein regulates. PAX2 and its interacting partner Pax transcription interacting protein recruit a histone methyltransferase complex to the promoter and epigentically regulate the expression of arginine vasopressin receptor 2, a protein that plays a crucial role in osmoregulation in the distal tubule.

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20

Jean, Ying Y., Elena M. Ribe, Maria Elena Pero, et al. "Caspase-2 is essential for c-Jun transcriptional activation and Bim induction in neuron death." Biochemical Journal 455, no. 1 (2013): 15–25. http://dx.doi.org/10.1042/bj20130556.

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Neuronal apoptotic death generally requires de novo transcription, and activation of the transcription factor c-Jun has been shown to be necessary in multiple neuronal death paradigms. Caspase-2 has been implicated in death of neuronal and non-neuronal cells, but its relationship to transcriptional activation has not been clearly elucidated. In the present study, using two different neuronal apoptotic paradigms, β-amyloid treatment and NGF (nerve growth factor) withdrawal, we examined the hierarchical role of caspase-2 activation in the transcriptional control of neuron death. Both paradigms i

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21

Miller, J., L. Fairall, and D. Rhodes. "A novel method for the purification of the Xenopus transcription factor IIIA." Nucleic Acids Research 17, no. 22 (1989): 9185–92. http://dx.doi.org/10.1093/nar/17.22.9185.

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Abstract We have developed a quick and simple purification method that yields large quantities of the Xenopus zinc finger protein transcription factor IIIA (TFIIIA). The protein is purified in the form of the 7S storage particle (TFIIIA/5S RNA complex) found in the ovaries of immature Xenopus. Our method yields 0.5 to 1 mg of pure 7S particle per ovary. It involves a high speed centrifugation step, fractionation on a gel filtration column and a precipitation step using calcium chloride. TFIIIA purified using this protocol retains full DNA binding activity and has the expected zinc ion content.

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22

Miang-Lon Ng, Patricia, and Thomas Lufkin. "Embryonic stem cells: protein interaction networks." BioMolecular Concepts 2, no. 1-2 (2011): 13–25. http://dx.doi.org/10.1515/bmc.2011.008.

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AbstractEmbryonic stem cells have the ability to differentiate into nearly all cell types. However, the molecular mechanism of its pluripotency is still unclear. Oct3/4, Sox2 and Nanog are important factors of pluripotency. Oct3/4 (hereafter referred to as Oct4), in particular, has been an irreplaceable factor in the induction of pluripotency in adult cells. Proteins interacting with Oct4 and Nanog have been identified via affinity purification and mass spectrometry. These data, together with iterative purifications of interacting proteins allowed a protein interaction network to be constructe

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23

Yang, Xiaojuan, Surendranath Baliji, R. Cody Buchmann, et al. "Functional Modulation of the Geminivirus AL2 Transcription Factor and Silencing Suppressor by Self-Interaction." Journal of Virology 81, no. 21 (2007): 11972–81. http://dx.doi.org/10.1128/jvi.00617-07.

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ABSTRACT The DNA genomes of geminiviruses have a limited coding capacity that is compensated for by the production of small multifunctional proteins. The AL2 protein encoded by members of the genus Begomovirus (e.g., Tomato golden mosaic virus) is a transcriptional activator, a silencing suppressor, and a suppressor of a basal defense. The related L2 protein of Beet curly top virus (genus Curtovirus) shares the pathogenicity functions of AL2 but lacks transcriptional activation activity. It is known that AL2 and L2 can suppress local silencing by interacting with adenosine kinase (ADK) and can

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24

Aronheim, A., E. Zandi, H. Hennemann, S. J. Elledge, and M. Karin. "Isolation of an AP-1 repressor by a novel method for detecting protein-protein interactions." Molecular and Cellular Biology 17, no. 6 (1997): 3094–102. http://dx.doi.org/10.1128/mcb.17.6.3094.

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Transcription factor AP-1 transduces environmental signals to the transcriptional machinery. To ensure a quick response yet maintain tight control over AP-1 target genes, AP-1 activity is likely to be negatively regulated in nonstimulated cells. To identify proteins that interact with the Jun subunits of AP-1 and repress its activity, we developed a novel screen for detecting protein-protein interactions that is not based on a transcriptional readout. In this system, the mammalian guanyl nucleotide exchange factor (GEF) Sos is recruited to the Saccharomyces cerevisiae plasma membrane harboring

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25

Pecorari, Rosalba, Francesca Bernassola, Gerry Melino, and Eleonora Candi. "Distinct interactors define the p63 transcriptional signature in epithelial development or cancer." Biochemical Journal 479, no. 12 (2022): 1375–92. http://dx.doi.org/10.1042/bcj20210737.

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The TP63 is an indispensable transcription factor for development and homeostasis of epithelia and its derived glandular tissue. It is also involved in female germline cell quality control, muscle and thymus development. It is expressed as multiple isoforms transcribed by two independent promoters, in addition to alternative splicing occurring at the mRNA 3′-UTR. Expression of the TP63 gene, specifically the amino-deleted p63 isoform, ΔNp63, is required to regulate numerous biological activities, including lineage specification, self-renewal capacity of epithelial stem cells, proliferation/exp

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26

Diakun, G. P., L. Fairall, and A. Klug. "EXAFS study of the zinc-binding sites in the protein transcription factor IIIA." Nature 324, no. 6098 (1986): 698–99. http://dx.doi.org/10.1038/324698a0.

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27

KLUG, A., J. MILLER, and A. D. McLACHLAN. "Repetitive Zn2+-binding domains in the protein transcription factor IIIA from Xenopus oocytes." Biochemical Society Transactions 14, no. 2 (1986): 221. http://dx.doi.org/10.1042/bst0140221a.

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28

Miller, J., A. D. McLachlan, and A. Klug. "Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes." EMBO Journal 4, no. 6 (1985): 1609–14. http://dx.doi.org/10.1002/j.1460-2075.1985.tb03825.x.

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29

Duan, Zhijun, Richard E. Person, Hu-Hui Lee, et al. "Epigenetic Regulation of Protein-Coding and MicroRNA Genes by the Gfi1-Interacting Tumor Suppressor PRDM5." Molecular and Cellular Biology 27, no. 19 (2007): 6889–902. http://dx.doi.org/10.1128/mcb.00762-07.

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ABSTRACT Gfi1 transcriptionally governs hematopoiesis, and its mutations produce neutropenia. In an effort to identify Gfi1-interacting proteins and also to generate new candidate genes causing neutropenia, we performed a yeast two-hybrid screen with Gfi1. Among other Gfi1-interacting proteins, we identified a previously uncharacterized member of the PR domain-containing family of tumor suppressors, PRDM5. PRDM5 has 16 zinc fingers, and we show that it acts as a sequence-specific, DNA binding transcription factor that targets hematopoiesis-associated protein-coding and microRNA genes, includin

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Jaspers, Pinja, Mikael Brosché, Kirk Overmyer, and Jaakko Kangasjär. "The transcription factor interacting protein RCD1 contains a novel conserved domain." Plant Signaling & Behavior 5, no. 1 (2010): 78–80. http://dx.doi.org/10.4161/psb.5.1.10293.

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31

Cho, Je-Yoel, Minjung Lee, Jung-Mo Ahn, et al. "Proteomic Analysis of a PDEF Ets Transcription Factor-Interacting Protein Complex." Journal of Proteome Research 8, no. 3 (2009): 1327–37. http://dx.doi.org/10.1021/pr800683b.

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32

Fang, Difeng, Rama Krishna Gurram, Kairong Cui, et al. "Bcl11b, a novel GATA3-interacting protein, regulates T-helper-2-cell differentiation and function." Journal of Immunology 198, no. 1_Supplement (2017): 223.13. http://dx.doi.org/10.4049/jimmunol.198.supp.223.13.

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Abstract GATA-binding protein 3 (GATA3) acts as the master transcription factor for type 2 T helper (Th2) cell differentiation and function. Fine-tuning GATA3 transcription activity is critical for effectively expelling extracellular parasites and preventing allergic disorders. However, it is still elusive how GATA3 function is regulated in Th2 cells. Here, we report that the transcription factor B-cell Lymphoma 11b (Bcl11b) is a novel component of the GATA3 transcriptional complex executing GATA3-mediated gene expression. Bcl11b binds to GATA3 through protein-protein interaction; ChIP-Seq ana

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33

Lieberson, Rebecca, Kerri A. Mowen, Kathryn D. McBride, et al. "Tumor Necrosis Factor Receptor–Associated Factor (Traf)2 Represses the T Helper Cell Type 2 Response through Interaction with Nfat-Interacting Protein (Nip45)." Journal of Experimental Medicine 194, no. 1 (2001): 89–98. http://dx.doi.org/10.1084/jem.194.1.89.

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Recently we have identified a novel protein NIP45 (nuclear factor of activated T cells [NFAT]-interacting protein) which substantially augments interleukin (IL)-4 gene transcription. The provision of NIP45 together with NFAT and the T helper cell type 2 (Th2)-specific transcription factor c-Maf to cells normally refractory to IL-4 production, such as B cells or Th1 clones, results in substantial IL-4 secretion to levels that approximate those produced by primary Th2 cells. In studies designed to further our understanding of NIP45 activity, we have uncovered a novel facet of IL-4 gene regulatio

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Ghosh, Hiyaa S., James V. Spencer, Bobby Ng, Michael W. McBurney та Paul D. Robbins. "Sirt1 interacts with transducin-like enhancer of split-1 to inhibit nuclear factor κB-mediated transcription". Biochemical Journal 408, № 1 (2007): 105–11. http://dx.doi.org/10.1042/bj20070817.

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Sirt1 is an NAD+-dependent deacetylase that plays a role in cellular processes such as transcriptional regulation, stress response, longevity and apoptosis. Sirt1 deacetylates histone proteins and certain transcription factors such as p53, CTIP2 (chicken ovalbumin upstream promoter-transcription factor-interacting protein 2), FOXO (forkhead box O) and NF-κB (nuclear factor κB). To identify potential Sirt1-interacting factors, we performed a yeast two-hybrid screen. The screen identified TLE1 (transducin-like enhancer of split-1) as a possible Sirt1-interacting factor, which was then confirmed

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35

Bryant, L. A., P. Mixon, M. Davidson, A. J. Bannister, T. Kouzarides, and J. H. Sinclair. "The Human Cytomegalovirus 86-Kilodalton Major Immediate-Early Protein Interacts Physically and Functionally with Histone Acetyltransferase P/CAF." Journal of Virology 74, no. 16 (2000): 7230–37. http://dx.doi.org/10.1128/jvi.74.16.7230-7237.2000.

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ABSTRACT The major immediate-early proteins of human cytomegalovirus (HCMV) play a pivotal role in controlling viral and cellular gene expression during productive infection. As well as negatively autoregulating its own promoter, the HCMV 86-kDa major immediate early protein (IE86) activates viral early gene expression and is known to be a promiscuous transcriptional regulator of cellular genes. IE86 appears to act as a multimodal transcription factor. It is able to bind directly to target promoters to activate transcription but is also able to bridge between upstream binding factors such as C

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36

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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Dolgikh, Alexandra Vyacheslavovna, and Elena A. Dolgikh. "Searching for regulators that interact with BELL1 transcription factor and control the legume-rhizobial symbiosis development." Ecological genetics 19, no. 1 (2021): 37–45. http://dx.doi.org/10.17816/ecogen51489.

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The development of nitrogen-fixing nodule, which is formed during legume-rhizobial symbiosis, requires the involvement of cell cycle regulators, phytohormones and homeodomain-containing transcription factors as well as other organogenesis processes. Along with homedomain-containing transcription factors from KNOX family, which participation in the control of nodule development has been studied recently, the role of transcription factors from BELL family in this process remains under-explored. At the same time, transcriptomic data for legumes shows an increase in the expression levels of genes

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38

Cho, Ssang-Goo, Anindita Bhoumik, Limor Broday, Vladimir Ivanov, Barry Rosenstein, and Ze'ev Ronai. "TIP49b, a Regulator of Activating Transcription Factor 2 Response to Stress and DNA Damage." Molecular and Cellular Biology 21, no. 24 (2001): 8398–413. http://dx.doi.org/10.1128/mcb.21.24.8398-8413.2001.

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ABSTRACT Activating transcription factor 2 (ATF2/CRE-BP1) is implicated in transcriptional control of stress-responsive genes. A yeast two-hybrid screen identified TBP-interacting protein 49b (TIP49b), a component of the INO80 chromatin-remodeling complex, as a novel ATF2-interacting protein. TIP49b's association with ATF2 is phosphorylation dependent and requires amino acids 150 to 248 of ATF2 (ATF2150–248), which are implicated in intramolecular inhibition of ATF2 transcriptional activities. Forced expression of TIP49b efficiently attenuated ATF2 transcriptional activities under normal growt

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Minoguchi, S., Y. Taniguchi, H. Kato, et al. "RBP-L, a transcription factor related to RBP-Jkappa." Molecular and Cellular Biology 17, no. 5 (1997): 2679–87. http://dx.doi.org/10.1128/mcb.17.5.2679.

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RBP-Jkappa is a sequence-specific DNA binding protein which plays a central role in signalling downstream of the Notch receptor by physically interacting with its intracellular region. Although at least four Notch genes exist in mammals, it is unknown whether each Notch requires a specific downstream signalling molecule. Here we report isolation and characterization of a mouse RBP-Jkappa-related gene named RBP-L that is expressed almost exclusively in lung, in contrast to the ubiquitous expression of RBP-Jkappa. For simplicity, we propose to call RBP-Jkappa RBP-J. The RBP-L protein bound to a

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Waardenberg, Ashley J., Bernou Homan, Stephanie Mohamed, Richard P. Harvey, and Romaric Bouveret. "Prediction and validation of protein–protein interactors from genome-wide DNA-binding data using a knowledge-based machine-learning approach." Open Biology 6, no. 9 (2016): 160183. http://dx.doi.org/10.1098/rsob.160183.

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The ability to accurately predict the DNA targets and interacting cofactors of transcriptional regulators from genome-wide data can significantly advance our understanding of gene regulatory networks. NKX2-5 is a homeodomain transcription factor that sits high in the cardiac gene regulatory network and is essential for normal heart development. We previously identified genomic targets for NKX2-5 in mouse HL-1 atrial cardiomyocytes using DNA-adenine methyltransferase identification (DamID). Here, we apply machine learning algorithms and propose a knowledge-based feature selection method for pre

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Wong, Matthew Man-Kin, Sancy Mary Joyson, Heiko Hermeking, and Sung Kay Chiu. "Transcription Factor AP4 Mediates Cell Fate Decisions: To Divide, Age, or Die." Cancers 13, no. 4 (2021): 676. http://dx.doi.org/10.3390/cancers13040676.

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Activating Enhancer-Binding Protein 4 (AP4)/transcription factor AP4 (TFAP4) is a basic-helix-loop-helix-leucine-zipper transcription factor that was first identified as a protein bound to SV40 promoters more than 30 years ago. Almost 15 years later, AP4 was characterized as a target of the c-Myc transcription factor, which is the product of a prototypic oncogene that is activated in the majority of tumors. Interestingly, AP4 seems to represent a central hub downstream of c-Myc and N-Myc that mediates some of their functions, such as proliferation and epithelial-mesenchymal transition (EMT). E

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Fang, Difeng, Kairong Cui, Gangqing Hu, et al. "Bcl11b, a novel GATA3-interacting protein, suppresses Th1 while limiting Th2 cell differentiation." Journal of Experimental Medicine 215, no. 5 (2018): 1449–62. http://dx.doi.org/10.1084/jem.20171127.

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GATA-binding protein 3 (GATA3) acts as the master transcription factor for type 2 T helper (Th2) cell differentiation and function. However, it is still elusive how GATA3 function is precisely regulated in Th2 cells. Here, we show that the transcription factor B cell lymphoma 11b (Bcl11b), a previously unknown component of GATA3 transcriptional complex, is involved in GATA3-mediated gene regulation. Bcl11b binds to GATA3 through protein–protein interaction, and they colocalize at many important cis-regulatory elements in Th2 cells. The expression of type 2 cytokines, including IL-4, IL-5, and

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Stanišić, Vladimir, Anna Malovannaya, Jun Qin, David M. Lonard та Bert W. O'Malley. "OTU Domain-containing Ubiquitin Aldehyde-binding Protein 1 (OTUB1) Deubiquitinates Estrogen Receptor (ER) α and Affects ERα Transcriptional Activity". Journal of Biological Chemistry 284, № 24 (2009): 16135–45. http://dx.doi.org/10.1074/jbc.m109.007484.

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Estrogen receptor (ER) α is an essential component in human physiology and is a key factor involved in the development of breast and endometrial cancers. ERα protein levels and transcriptional activity are tightly controlled by the ubiquitin proteasome system. Deubiquitinating enzymes, a class of proteases capable of removing ubiquitin from proteins, are increasingly being seen as key modulators of the ubiquitin proteasome system, regulating protein stability and other functions by countering the actions of ubiquitin ligases. Using mass spectrometry analysis of an ERα protein complex, we ident

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McNabb, David S., and Inés Pinto. "Assembly of the Hap2p/Hap3p/Hap4p/Hap5p-DNA Complex in Saccharomyces cerevisiae." Eukaryotic Cell 4, no. 11 (2005): 1829–39. http://dx.doi.org/10.1128/ec.4.11.1829-1839.2005.

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ABSTRACT The CCAAT-binding factor (CBF) is an evolutionarily conserved multimeric transcriptional activator in eukaryotes. In Saccharomyces cerevisiae, the CCAAT-binding factor is composed of four subunits, termed Hap2p, Hap3p, Hap4p, and Hap5p. The Hap2p/Hap3p/Hap5p heterotrimer is the DNA-binding component of the complex that binds to the consensus 5′-CCAAT-3′ sequence in the promoter of target genes. The Hap4p subunit contains the transcriptional activation domain necessary for stimulating transcription after interacting with Hap2p/Hap3p/Hap5p. In this report, we demonstrate that Hap2p, Hap

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Mathieu, O. "Identification and characterization of transcription factor IIIA and ribosomal protein L5 from Arabidopsis thaliana." Nucleic Acids Research 31, no. 9 (2003): 2424–33. http://dx.doi.org/10.1093/nar/gkg335.

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Choudhry, M. A., and I. J. McEwan. "In vitro regulation of reporter gene transcription by the androgen receptor AF1 domain." Biochemical Society Transactions 32, no. 6 (2004): 1103–6. http://dx.doi.org/10.1042/bst0321103.

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The androgen receptor (AR) is a ligand-activated transcription factor that regulates gene expression in response to the steroids testosterone and dihydrotestosterone. AR-dependent gene expression is likely to play an important role in a number of receptor-associated disorders, such as prostate cancer, spinal bulbar muscular atrophy, male type baldness and hirsutism. The AR contains two transactivation domains, termed AF1 (activation function 1) located in the N-terminus and AF2 (activation function 2) in the C-terminal ligand-binding domain. AF2 exhibits weak transcriptional activity, whereas

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Cai, Ying, Zhixiong Xu, Jingping Xie, Mark J. Koury, Scott W. Hiebert, and Stephen J. Brandt. "Proteomic Identification of TAL1/SCL-Interacting Proteins: ETO-2 and MTGR1 Interact with TAL1 in Erythroid Progenitors." Blood 104, no. 11 (2004): 357. http://dx.doi.org/10.1182/blood.v104.11.357.357.

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Abstract The TAL1/SCL gene, originally identified from its involvement by a recurrent chromosomal translocation in T-cel acute lymphoblastic leukemia, encodes a basic helix-loop-helix (bHLH) transcription factor essential for hematopoietic and vascular development. Although TAL1 is believed to regulate transcription of specific sets of target genes, the mechanisms underlying TAL1-directed gene expression are poorly understood. Previous studies have shown, in fact, that it can act as either an activator or repressor depending on the coregulator(s) with which it interacts. To comprehensively ide

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Encarnacao, Priscilla C., Vincent P. Ramirez, Carmen Zhang та Brian J. Aneskievich. "Sp sites contribute to basal and inducible expression of the human TNIP1 (TNFα-inducible protein 3-interacting protein 1) promoter". Biochemical Journal 452, № 3 (2013): 519–29. http://dx.doi.org/10.1042/bj20121666.

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TNIP1 [TNFα (tumour necrosis factor α)-induced protein 3-interacting protein 1] is a co-repressor of RAR (retinoic acid receptor) and PPAR (peroxisome-proliferator-activated receptor). Additionally, it can reduce signalling stemming from cell membrane receptors such as those for TNFα and EGF (epidermal growth factor). Consequently, it influences a variety of receptor-mediated events as diverse as transcription, programmed cell death and cell cycling. Thus changes in TNIP1 expression levels are likely to affect multiple important biological end points. TNIP1 expression level changes have been l

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Daruliza Kernain and Shaharum Shamsuddin. "Interaction between Two Transcriptional Factors CTCF and YB-1 – Truncated domains in Brain Cancer Cell line." International Journal of Research in Pharmaceutical Sciences 10, no. 4 (2019): 3332–38. http://dx.doi.org/10.26452/ijrps.v10i4.1642.

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CTCF is a protein involved in the regulation of transcription, insulator function, and the X-chromosome inactivation. It is an 11 ZF transcriptional factor which is highly conserved between the species. Identification of proteins interacting with CTCF can help to elucidate the function in the cell. Previously reported studies had identified numerous CTCF protein interacting partners, and one of the interacting partners chosen in this study is YB-1. Brain cancer cell –RGBM was selected as a model to study the interaction between CTCF and YB-1. Firstly, proteins were transformed and expressed in

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Dorjsuren, Dorjbal, Yong Lin, Wenxiang Wei, et al. "RMP, a Novel RNA Polymerase II Subunit 5-Interacting Protein, Counteracts Transactivation by Hepatitis B Virus X Protein." Molecular and Cellular Biology 18, no. 12 (1998): 7546–55. http://dx.doi.org/10.1128/mcb.18.12.7546.

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ABSTRACT To modulate transcription, regulatory factors communicate with basal transcription factors and/or RNA polymerases in a variety of ways. Previously, it has been reported that RNA polymerase II subunit 5 (RPB5) is one of the targets of hepatitis B virus X protein (HBx) and that both HBx and RPB5 specifically interact with general transcription factor IIB (TFIIB), implying that RPB5 is one of the communicating subunits of RNA polymerase II involved in transcriptional regulation. In this context, we screened for a host protein(s) that interacts with RPB5. By far-Western blot screening, we

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