The S1 RNA-binding domain is a protein domain found in many RNA-associated proteins, named after its original identification in ribosomal protein S1. It is a reusable RNA-interaction module; its presence does not identify the entire host protein as a ribosomal component or a nuclease.[ref]
The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold by M. Bycroft and others. Abstract: origin of the domain name and occurrence in RNA-associated proteins
A 1997 structural experiment examined the S1 domain of Escherichia coli polynucleotide phosphorylase using nuclear magnetic resonance. The resulting structure was a five-stranded antiparallel beta barrel. Conserved residues on one face and neighboring loops suggested an RNA-binding surface; that proposal distinguished an observed fold from an inferred contact function.[ref]
The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold by M. Bycroft and others. Abstract: NMR structure and putative binding face
The 2016 RNase R study supplies a functional example. Altering residues in its S1 domain changed interactions with duplex RNA, while separate measurements examined nucleotide binding, conformational changes and degradation. A binding domain can therefore influence catalysis by positioning a substrate or stabilizing a productive state, without itself supplying all catalytic chemistry.[ref]
For an architectural counting example, a hypothetical protein with two S1 domains has two copies of that module, not automatically two RNA-cleaving active sites. Domain count, binding behavior and enzyme activity are different observations that require different evidence.
Articles by others on the same topic
There are currently no matching articles.