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S1 RNA-binding domain-containing protein
The S1 domain occurs in a wide range of RNA associated proteins. It is structurally similar to cold shock protein which binds nucleic acids. The S1 domain has an OB-fold structure. Structure and an extension of S1 family. [1]. 9008164. The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold. Bycroft M, Hubbard TJ, Proctor M, Freund SM, Murzin AG;. Cell 1997;88:235-242. (from Pfam)
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator
CvfD, Ygs, and GSP13 form a family of full-length homologs of RNA-binding proteins from the Firmicutes with a single copy of the S1 domain. Several members of the family have been characterized as general stress proteins, and the most recently characterized, CvfD, was shown to act as a post-transcriptional regulator.
S1 domain-containing post-transcriptional regulator Ygs
Ygs, as first described in Staphylococcus epidermidis, is a full-length homolog of GSP13 (YugI) from Bacillus subtilis. Each has a single copy of the S1 domain, an RNA-binding domain repeated several times in ribosomal small subunit protein S1, and each has been shown to be induced by stress and improve survival. Ygs was shown in Staphylococcus epidermidis to affect polysaccharide intercellular adhesin biosynthesis, and through it, biofilm formation. More recently, the full-length homolog CvfD was shown to be a post-transcriptional regulator, suggesting all members of this family are.
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