scholarly journals The insulator functions of the Drosophila polydactyl C2H2 zinc finger protein CTCF: Necessity versus sufficiency

2020 ◽  
Vol 6 (13) ◽  
pp. eaaz3152
Author(s):  
Olga Kyrchanova ◽  
Oksana Maksimenko ◽  
Airat Ibragimov ◽  
Vladimir Sokolov ◽  
Nikolay Postika ◽  
...  
Keyword(s):  
Zinc Finger ◽  
Binding Sites ◽  
Zinc Finger Protein ◽  
Gene Clusters ◽  
Recognition Sequence ◽  
C2h2 Zinc Finger ◽  
Insulator Activity ◽  
Dna Binding Factors ◽  
Chromosomal Architecture ◽  
Functional Boundary

In mammals, a C2H2 zinc finger (C2H2) protein, CTCF, acts as the master regulator of chromosomal architecture and of the expression of Hox gene clusters. Like mammalian CTCF, the Drosophila homolog, dCTCF, localizes to boundaries in the bithorax complex (BX-C). Here, we have determined the minimal requirements for the assembly of a functional boundary by dCTCF and two other C2H2 zinc finger proteins, Pita and Su(Hw). Although binding sites for these proteins are essential for the insulator activity of BX-C boundaries, these binding sites alone are insufficient to create a functional boundary. dCTCF cannot effectively bind to a single recognition sequence in chromatin or generate a functional insulator without the help of additional proteins. In addition, for boundary elements in BX-C at least four binding sites for dCTCF or the presence of additional DNA binding factors is required to generate a functional insulator.

scholarly journals The Cardiac Tissue-Restricted Homeobox Protein Csx/Nkx2.5 Physically Associates with the Zinc Finger Protein GATA4 and Cooperatively Activates Atrial Natriuretic Factor Gene Expression

1998 ◽  
Vol 18 (6) ◽  
pp. 3120-3129 ◽  
Author(s):  
Youngsook Lee ◽  
Tetsuo Shioi ◽  
Hideko Kasahara ◽  
Shawn M. Jobe ◽  
Russell J. Wiese ◽  
...  
Keyword(s):  
Gene Expression ◽  
Zinc Finger ◽  
Protein Interaction ◽  
Binding Sites ◽  
Atrial Natriuretic Factor ◽  
Target Gene ◽  
Cardiac Tissue ◽  
Zinc Finger Protein ◽  
Finger Protein ◽  
Homeobox Protein

ABSTRACT Specification and differentiation of the cardiac muscle lineage appear to require a combinatorial network of many factors. The cardiac muscle-restricted homeobox protein Csx/Nkx2.5 (Csx) is expressed in the precardiac mesoderm as well as the embryonic and adult heart. Targeted disruption of Csx causes embryonic lethality due to abnormal heart morphogenesis. The zinc finger transcription factor GATA4 is also expressed in the heart and has been shown to be essential for heart tube formation. GATA4 is known to activate many cardiac tissue-restricted genes. In this study, we tested whether Csx and GATA4 physically associate and cooperatively activate transcription of a target gene. Coimmunoprecipitation experiments demonstrate that Csx and GATA4 associate intracellularly. Interestingly, in vitro protein-protein interaction studies indicate that helix III of the homeodomain of Csx is required to interact with GATA4 and that the carboxy-terminal zinc finger of GATA4 is necessary to associate with Csx. Both regions are known to directly contact the cognate DNA sequences. The promoter-enhancer region of the atrial natriuretic factor (ANF) contains several putative Csx binding sites and consensus GATA4 binding sites. Transient-transfection assays indicate that Csx can activate ANF reporter gene expression to the same extent that GATA4 does in a DNA binding site-dependent manner. Coexpression of Csx and GATA4 synergistically activates ANF reporter gene expression. Mutational analyses suggest that this synergy requires both factors to fully retain their transcriptional activities, including the cofactor binding activity. These results demonstrate the first example of homeoprotein and zinc finger protein interaction in vertebrates to cooperatively regulate target gene expression. Such synergistic interaction among tissue-restricted transcription factors may be an important mechanism to reinforce tissue-specific developmental pathways.

scholarly journals Comprehensive genomic survey, structural classification and expression analysis of C2H2 zinc finger protein gene family in Brassica rapa L.

PLoS ONE ◽  
2019 ◽  
Vol 14 (5) ◽  
pp. e0216071 ◽  
Author(s):  
Intikhab Alam ◽  
Khadija Batool ◽  
Dong-Li Cui ◽  
Yan-Qing Yang ◽  
Yun-Hai Lu
Keyword(s):  
Gene Family ◽  
Zinc Finger ◽  
Brassica Rapa ◽  
Expression Analysis ◽  
Protein Gene ◽  
Zinc Finger Protein ◽  
Structural Classification ◽  
C2h2 Zinc Finger ◽  
Zinc Finger Protein Gene ◽  
Finger Protein

A novel C2H2 zinc-finger protein gene (ZNF160) maps to human chromosome 19q13.3–q13.4

Genomics ◽  
1995 ◽  
Vol 25 (1) ◽  
pp. 322-323 ◽  
Author(s):  
Stephanie Halford ◽  
Marie-Genevieve Mattei ◽  
Sara Daw ◽  
Peter J. Scambler
Keyword(s):  
Human Chromosome ◽  
Zinc Finger ◽  
Protein Gene ◽  
Zinc Finger Protein ◽  
C2h2 Zinc Finger ◽  
Zinc Finger Protein Gene ◽  
Finger Protein ◽  
C2h2 Zinc Finger Protein

Abstract 2392: Transcriptional repression of VEGF by Znf24, a C2H2 zinc finger protein

2010 ◽  
Author(s):  
Di Jia ◽  
Robyn Loureiro ◽  
Patricia D'Amore ◽  
Scott Rodig ◽  
Marsha Moses
Keyword(s):  
Zinc Finger ◽  
Transcriptional Repression ◽  
Zinc Finger Protein ◽  
C2h2 Zinc Finger ◽  
Finger Protein ◽  
C2h2 Zinc Finger Protein

scholarly journals ZNF300, a recently identified human transcription factor, activates the human IL-2Rβ promoter through the overlapping ZNF300/EGR1 binding site

2010 ◽  
Vol 15 (4) ◽  
Author(s):  
Lu Xue ◽  
Hongling Qiu ◽  
Jian Ma ◽  
Mingxiong Guo ◽  
Wenxin Li
Keyword(s):  
Binding Site ◽  
Zinc Finger ◽  
Zinc Finger Protein ◽  
Protein Family ◽  
Binding Property ◽  
Mobility Shift ◽  
Transient Transfection Assay ◽  
C2h2 Zinc Finger ◽  
Finger Protein ◽  
C2h2 Zinc Finger Protein

AbstractZNF300 was recently identified as a member of the human KRAB/C2H2 zinc finger protein family. Little is known about the role of ZNF300 in human gene regulation networks. In this study, the DNA-binding property of ZNF300 was further analyzed. We found that the recombinant ZNF300 could bind to the binding site 5′-GCGGGGGCG-3′ of Egr1, another member of the KRAB/C2H2 zinc finger protein family. Similarly, recombinant Egr1 also showed a similar binding affinity to the ZNF300 binding site 5′-CTGGGGGCG-3′. Bioinformatics analysis revealed that there is an overlapping ZNF300/Egr1 binding site in the human IL-2Rβ promoter region, which was previously known to be recognized by endogenous Egr1. Electrophoretic mobility shift assays showed that endogenous ZNF300 could also bind to this site. A transient transfection assay revealed that both ZNF300 and Egr1 could transactivate the IL-2Rβ promoter, and that the activation was abrogated by a mutation of residues in the overlapping ZNF300/Egr1 binding site. Co-expression of ZNF300 and Egr1 led to enhanced IL-2Rβ promoter activity. Thus, ZNF300 is likely to be another regulator of the human IL-2Rβ promoter.

TvZNF1 is a C2H2 zinc finger protein of Trichomonas vaginalis

BioMetals ◽  
2017 ◽  
Vol 30 (6) ◽  
pp. 861-872 ◽  
Author(s):  
José Luis Villalpando ◽  
Rodrigo Arreola ◽  
Jonathan Puente-Rivera ◽  
Elisa Azuara-Liceaga ◽  
Jesús Valdés ◽  
...  
Keyword(s):  
Zinc Finger ◽  
Trichomonas Vaginalis ◽  
Zinc Finger Protein ◽  
C2h2 Zinc Finger ◽  
Finger Protein ◽  
C2h2 Zinc Finger Protein
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