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PMID: 10675344 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Structure of Hsp15 reveals a novel RNA-binding motif.

The EMBO journal ·Vol. 19 ·No. 4 ·2000-02-15 ·Pages 749-57

Staker BL, Korber P, Bardwell JC, Saper MA

Abstract

We have solved the crystal structure of the heat shock protein Hsp15, a newly isolated and very highly inducible heat shock protein that binds the ribosome. Comparison of its structure with those of two RNA-binding proteins, ribosomal protein S4 and threonyl-tRNA synthetase, reveals a novel RNA-binding motif. This newly recognized motif is remarkably common, present in at least eight different protein families that bind RNA. The motif's surface is populated by conserved, charged residues that define a likely RNA-binding site. An intriguing pattern emerges: stress proteins, ribosomal proteins and tRNA synthetases repeatedly share a conserved motif. This may imply a hitherto unrecognized functional similarity between these three protein classes.

MeSH Terms
Amino Acid Motifs Amino Acid Sequence Bacterial Proteins/chemistry,genetics,metabolism Binding Sites Conserved Sequence Crystallography, X-Ray DNA-Binding Proteins/chemistry,genetics,metabolism Escherichia coli/chemistry,genetics,metabolism Escherichia coli Proteins Heat-Shock Proteins/chemistry,genetics,metabolism Models, Molecular Molecular Sequence Data Protein Conformation Protein Structure, Secondary Protein Structure, Tertiary RNA-Binding Proteins/chemistry,genetics,metabolism Ribosomal Proteins/chemistry,genetics Threonine-tRNA Ligase/chemistry,genetics
Chemicals
Bacterial Proteins DNA-Binding Proteins Escherichia coli Proteins Heat-Shock Proteins RNA-Binding Proteins Ribosomal Proteins hslR protein, E coli ribosomal protein S4 Threonine-tRNA Ligase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Staker B L
Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
Korber P
Bardwell J C
Saper M A
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
DOI
10.1093/emboj/19.4.749
Published
2000-02-15
Pages
749-57
Language
English
Region
England
NLM ID
8208664
PMCID
PMC305613
Subset
IM
External Links
PubMed source DOI: 10.1093/emboj/19.4.749 PMC Full Text View journal details
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