Disease relevance of Sry-beta

• They are determinant for specific binding of the sry beta and delta proteins, respectively, produced in Escherichia coli or present in Drosophila embryos [1].

High impact information on Sry-beta

• The consensus recognition sites sry beta 5'-YCAGAGATGCGCA-3' and sry delta 5'-YTAGAGATGGRAA-3' thus differ by nucleotides at four out of 13 positions [1].
• Two out of the five characterized in detail map at cytological positions coincident with binding sites of the native sry beta protein on polytene chromosomes [1].
• Both the sry beta and delta proteins protect an 18-22 base region from DNase I digestion within each analysed genomic binding site, that includes a 13 bp consensus sequence [1].
• The identified sry beta genomic targets are all contained within single-copy DNA in euchromatic regions of the genome [1].
• The closely related Drosophila serendipity (sry) beta and delta zinc finger proteins display consensus in vitro DNA recognition sequences differing by 4 of 13 nucleotide positions and bind in vivo to distinct sets of sites on polytene chromosomes [2].

Biological context of Sry-beta

• The genes janus (jan) A and B, and serendipity (sry) beta and delta are two pairs of duplicated genes that are adjacent to each other on the third chromosome of Drosophila melanogaster [3].
• Zinc fingers and other domains cooperate in binding of Drosophila sry beta and delta proteins at specific chromosomal sites [2].
• Zygotic synthesis of the sry beta protein starts during nuclear division cycles 12-13, prior to cellularisation of the blastoderm, while the zygotic sry delta protein is not detectable before germ band extension (stage 10 embryos) [4].
• The data indicate that the five different (and partially overlapping) sry messenger RNAs detectable in early embryos are initiated at three separate sites, each directly upstream from one of the three protein-coding regions, designated (in 5' to 3' order) beta, alpha and delta [5].
• The Drosophila serendipity (sry) beta and delta genes, which resulted from a gene duplication event, provide an interesting model for the evolutionary diversification in structure and function of C2H2 zinc finger proteins [6].

Associations of Sry-beta with chemical compounds

• The NH2-terminal region and fingers 1, 5, and 6 differentiate the sry beta and delta proteins while zinc fingers 2, 3, and 4 are virtually identical in these two paralogs [6].

Other interactions of Sry-beta

• Our results show that sry beta cis-acting sequences are located in the (-117; +137) 5'-region of the gene and that jan A cis-regulatory sequences are included in the (-56; +151) 5'-domain of this gene [3].

References