Evidence that E. coli ribosomal protein S13 has two separable functional domains involved in 16S RNA recognition and protein S19 binding.

Evidence that E. coli ribosomal protein S13 has two separable functional domains involved in 16S RNA recognition and protein S19 binding.

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MedLine Citation:	PMID: 3903659 Owner: NLM Status: MEDLINE
Abstract/OtherAbstract:	We have found that E. coli ribosomal protein S13 recognizes multiple sites on 16S RNA. However, when protein S19 is included with a mixture of proteins S4, S7, S8, S16/S17 and S20, the S13 binds to the complex with measurably greater strength and with a stoichiometry of 1.5 copies per particle. This suggests that the protein may have two functional domains. We have tested this idea by cleaving the protein into two polypeptides. It was found that one of the fragments, composed of amino acid residues 84-117, retained the capacity to bind 16S RNA at multiple sites. Protein S19 had no affect on the strength or stoichiometry of the binding of this fragment. These data suggest that S13 has a C-terminal domain primarily responsible for RNA recognition and possibly that the N-terminal region is important for association with protein S19.

Authors:	J Schwarzbauer; G R Craven
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Publication Detail:	Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
Journal Detail:	Title: Nucleic acids research Volume: 13 ISSN: 0305-1048 ISO Abbreviation: Nucleic Acids Res. Publication Date: 1985 Sep
Date Detail:	Created Date: 1985-11-27 Completed Date: 1985-11-27 Revised Date: 2009-11-18
Medline Journal Info:	Nlm Unique ID: 0411011 Medline TA: Nucleic Acids Res Country: ENGLAND
Other Details:	Languages: eng Pagination: 6767-86 Citation Subset: IM
Export Citation:	APA/MLA Format Download EndNote Download BibTex
MeSH Terms
Descriptor/Qualifier:	Amino Acids / analysis Binding Sites Centrifugation, Density Gradient Electrophoresis, Polyacrylamide Gel Escherichia coli / genetics, metabolism* Escherichia coli Proteins Kinetics Macromolecular Substances Molecular Weight Peptide Fragments / analysis Protein Binding RNA, Ribosomal / metabolism* Ribosomal Proteins / metabolism* Ribosomes / metabolism*
Grant Support
ID/Acronym/Agency:	GM-24019/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:	0/Amino Acids; 0/Escherichia coli Proteins; 0/Macromolecular Substances; 0/Peptide Fragments; 0/RNA, Ribosomal; 0/Ribosomal Proteins; 0/ribosomal protein S19; 0/rpsM protein, E coli
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Journal Information Journal ID (nlm-ta): Nucleic Acids Res ISSN: 0305-1048 ISSN: 1362-4962	Article Information Download PDF Print publication date: Day: 25 Month: 9 Year: 1985 Volume: 13 Issue: 18 First Page: 6767 Last Page: 6786 ID: 321992 PubMed Id: 3903659