Faculty Opinions recommendation of Expanding the DNA-recognition repertoire for zinc finger proteins beyond 20 amino acids.

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.

Download Full-text

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

Molecular and Cellular Biology ◽

10.1128/mcb.10.1.418-421.1990 ◽

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.

Download Full-text

A Theoretical Study of the Physicochemical Mechanisms Associated with DNA Recognition Modulation in Artificial Zinc-Finger Proteins

The Journal of Physical Chemistry B ◽

10.1021/jp1097348 ◽

2011 ◽

Vol 115 (16) ◽

pp. 4774-4780 ◽

Cited By ~ 10

Author(s):

Hirotoshi Mori ◽

Kaori Ueno-Noto

Keyword(s):

Zinc Finger ◽

Theoretical Study ◽

Dna Recognition ◽

Zinc Finger Proteins

Download Full-text

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

Molecular and Cellular Biology ◽

10.1128/mcb.15.6.3424 ◽

1995 ◽

Vol 15 (6) ◽

pp. 3424-3429 ◽

Cited By ~ 42

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.

Download Full-text