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- W1967161878 endingPage "628" @default.
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- W1967161878 abstract "Maternally expressed Skn-1 protein is required for the correct specification of certain blastomere fates in early Caenorhabditis elegans embryos. Skn-1 contains a basic region similar to those of basic leucine zipper (bZIP) proteins but, paradoxically, it lacks a leucine zipper dimerization segment. Random sequence selection methods were used to show that Skn-1 binds to specific DNA sequences as a monomer. The Skn-1 basic region lies at the carboxyl terminus of an 85-amino acid domain that binds preferentially to a bZIP half-site and also recognizes adjacent 5′ AT-rich sequences in the minor groove, apparently with an amino (NH2)-terminal arm related to those of homeodomain proteins. The intervening residues appear to stabilize interactions of these two subdomains with DNA. The Skn-1 DNA binding domain thus represents an alternative strategy for promoting binding of a basic region segment recognition helix to its cognate half-site. The results point to an underlying modularity in subdomains within established DNA binding domains." @default.
- W1967161878 created "2016-06-24" @default.
- W1967161878 creator A5039596752 @default.
- W1967161878 creator A5054807857 @default.
- W1967161878 creator A5066849551 @default.
- W1967161878 creator A5088001169 @default.
- W1967161878 date "1994-10-28" @default.
- W1967161878 modified "2023-10-09" @default.
- W1967161878 title "Formation of a Monomeric DNA Binding Domain by Skn-1 bZIP and Homeodomain Elements" @default.
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- W1967161878 doi "https://doi.org/10.1126/science.7939715" @default.
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