scholarly journals A gene that encodes a protein consisting solely of zinc finger domains is preferentially expressed in transformed mouse cells.

1990 ◽  
Vol 10 (1) ◽  
pp. 418-421 ◽  
Author(s):  
M Ernoult-Lange ◽  
M Kress ◽  
D Hamer
Keyword(s):  
Amino Acids ◽  
Brain Tissue ◽  
Zinc Finger ◽  
Cellular Transformation ◽  
Zinc Finger Proteins ◽  
Mouse Cells ◽  
Zinc Finger Domains ◽  
Transformed Cell Lines ◽  
Testis Tissue

We describe the cloning and characterization of the mouse MOK-2 gene, a new member of the Krüppel family of zinc finger proteins. Sequencing of both cDNA and genomic clones showed that the predicted MOK-2 protein consists of seven zinc finger domains with only five additional amino acids. The finger domains of MOK-2 are highly homologous to one another but not to those of other zinc finger proteins. MOK-2 is preferentially expressed in transformed cell lines, brain tissue, and testis tissue. Its possible role in cellular transformation is discussed.

A gene that encodes a protein consisting solely of zinc finger domains is preferentially expressed in transformed mouse cells

1990 ◽  
Vol 10 (1) ◽  
pp. 418-421
Author(s):  
M Ernoult-Lange ◽  
M Kress ◽  
D Hamer
Keyword(s):  
Amino Acids ◽  
Brain Tissue ◽  
Zinc Finger ◽  
Cellular Transformation ◽  
Zinc Finger Proteins ◽  
Mouse Cells ◽  
Zinc Finger Domains ◽  
Transformed Cell Lines ◽  
Testis Tissue

We describe the cloning and characterization of the mouse MOK-2 gene, a new member of the Krüppel family of zinc finger proteins. Sequencing of both cDNA and genomic clones showed that the predicted MOK-2 protein consists of seven zinc finger domains with only five additional amino acids. The finger domains of MOK-2 are highly homologous to one another but not to those of other zinc finger proteins. MOK-2 is preferentially expressed in transformed cell lines, brain tissue, and testis tissue. Its possible role in cellular transformation is discussed.

Functional characterization of rice CW-domain containing zinc finger proteins involved in histone recognition

Plant Science ◽  
2017 ◽  
Vol 263 ◽  
pp. 168-176 ◽  
Author(s):  
Zhe Zhang ◽  
Feng Zhang ◽  
Zhi-jun Cheng ◽  
Ling-long Liu ◽  
Qi-bing Lin ◽  
...  
Keyword(s):  
Zinc Finger ◽  
Functional Characterization ◽  
Zinc Finger Proteins

Cloning and comparative analysis of the bovine, porcine, and equine sex chromosome genes ZFX and ZFY

Genome ◽  
2004 ◽  
Vol 47 (1) ◽  
pp. 74-83 ◽  
Author(s):  
Arkadi Poloumienko
Keyword(s):  
Amino Acids ◽  
Zinc Finger ◽  
Sex Chromosome ◽  
Zinc Finger Proteins ◽  
Mammalian Development ◽  
Coding Regions ◽  
Zinc Finger Motifs ◽  
Internal Exon ◽  
Alternatively Spliced ◽  
Zfy Genes

A growing body of evidence suggests the involvement of sex chromosome genes in mammalian development. We report the cloning and characterization of the complete coding regions of the bovine Y chromosome ZFY and X chromosome ZFX genes, and partial coding regions of porcine and equine ZFX and ZFY genes. Bovine ZFY and ZFX are highly similar to each other and to ZFX and ZFY from other species. While bovine and human ZFY proteins are both 801 amino acids long, bovine ZFX is 5 amino acids shorter than human ZFX. Like in humans, both bovine ZFY and ZFX contain 13 zinc finger motifs and belong to the Krueppel family of C2H2-type zinc finger proteins. The internal exon–intron organization of the bovine, porcine and equine ZFX and ZFY genes has been determined and compared. Within this region, the exon lengths and the positions of the splice sites are conserved, further suggesting a high evolutionary conservation of the ZFX and ZFY genes. Additionally, new alternatively spliced forms of human ZFX have been identified.Key words: sex chromosome genes, zinc finger proteins, ZFX, ZFY, alternative splicing.

scholarly journals Characterization of the ZFX family of transcription factors that bind downstream of the start site of CpG island promoters

2020 ◽  
Vol 48 (11) ◽  
pp. 5986-6000 ◽  
Author(s):  
Weiya Ni ◽  
Andrew A Perez ◽  
Shannon Schreiner ◽  
Charles M Nicolet ◽  
Peggy J Farnham
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Cpg Island ◽  
Zinc Finger Proteins ◽  
Double Knockout ◽  
Altered Expression ◽  
C2h2 Zinc Finger ◽  
Necessary And Sufficient ◽  
Functional Analyses

Abstract Our study focuses on a family of ubiquitously expressed human C2H2 zinc finger proteins comprised of ZFX, ZFY and ZNF711. Although their protein structure suggests that ZFX, ZFY and ZNF711 are transcriptional regulators, the mechanisms by which they influence transcription have not yet been elucidated. We used CRISPR-mediated deletion to create bi-allelic knockouts of ZFX and/or ZNF711 in female HEK293T cells (which naturally lack ZFY). We found that loss of either ZFX or ZNF711 reduced cell growth and that the double knockout cells have major defects in proliferation. RNA-seq analysis revealed that thousands of genes showed altered expression in the double knockout clones, suggesting that these TFs are critical regulators of the transcriptome. To gain insight into how these TFs regulate transcription, we created mutant ZFX proteins and analyzed them for DNA binding and transactivation capability. We found that zinc fingers 11–13 are necessary and sufficient for DNA binding and, in combination with the N terminal region, constitute a functional transactivator. Our functional analyses of the ZFX family provides important new insights into transcriptional regulation in human cells by members of the large, but under-studied family of C2H2 zinc finger proteins.

Solution structures and characterization of human immunodeficiency virus Rev responsive element IIB RNA targeting zinc finger proteins

Biopolymers ◽  
2006 ◽  
Vol 83 (4) ◽  
pp. 352-364 ◽  
Author(s):  
Subrata H. Mishra ◽  
Christopher M. Shelley ◽  
Doyle J. Barrow ◽  
Martyn K. Darby ◽  
Markus W. Germann
Keyword(s):  
Human Immunodeficiency Virus ◽  
Zinc Finger ◽  
Zinc Finger Proteins ◽  
Solution Structures ◽  
Rna Targeting ◽  
Immunodeficiency Virus ◽  
Responsive Element

scholarly journals Co(II) Coordination in Prokaryotic Zinc Finger Domains as Revealed by UV-Vis Spectroscopy

2017 ◽  
Vol 2017 ◽  
pp. 1-7 ◽  
Author(s):  
Valeria Sivo ◽  
Gianluca D’Abrosca ◽  
Luigi Russo ◽  
Rosa Iacovino ◽  
Paolo Vincenzo Pedone ◽  
...  
Keyword(s):  
Zinc Finger ◽  
Coordination Sphere ◽  
Metal Ion ◽  
Electronic Configuration ◽  
Transition Band ◽  
Tetrahedral Geometry ◽  
Vis Spectroscopy ◽  
Zinc Finger Domains ◽  
Spectroscopic Probe

Co(II) electronic configuration allows its use as a spectroscopic probe in UV-Vis experiments to characterize the metal coordination sphere that is an essential component of the functional structure of zinc-binding proteins and to evaluate the metal ion affinities of these proteins. Here, exploiting the capability of the prokaryotic zinc finger to use different combinations of residues to properly coordinate the structural metal ion, we provide the UV-Vis characterization of Co(II) addition to Ros87 and its mutant Ros87_C27D which bears an unusual CysAspHis2 coordination sphere. Zinc finger sites containing only one cysteine have been infrequently characterized. We show for the CysAspHis2 coordination an intense d-d transition band, blue-shifted with respect to the Cys2His2 sphere. These data complemented by NMR and CD data demonstrate that the tetrahedral geometry of the metal site is retained also in the case of a single-cysteine coordination sphere.

scholarly journals The BTB domain of bric à brac mediates dimerization in vitro.

1995 ◽  
Vol 15 (6) ◽  
pp. 3424-3429 ◽  
Author(s):  
W Chen ◽  
S Zollman ◽  
J L Couderc ◽  
F A Laski
Keyword(s):  
Amino Acids ◽  
Drosophila Melanogaster ◽  
Amino Acid ◽  
Zinc Finger ◽  
Zinc Finger Proteins ◽  
Protein Dimerization ◽  
Conserved Motif ◽  
Btb Domain

The gene bric à brac (bab) is required for the proper development of the limbs and ovary in Drosophila melanogaster. bab encodes a BTB domain (also called a POZ domain), an approximately 115-amino-acid conserved motif found primarily in the N termini of zinc finger proteins. In this paper, we show that the BTB domain of bab can mediate protein dimerization in vitro. In addition, we demonstrate that the first 51 amino acids of the bab BTB domain are sufficient for dimerization, and we identify amino acids within this region that are required for binding.

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