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Structure of Hsp15 reveals a novel RNA‐binding motif
Author(s) -
Staker Bart L.,
Korber Philipp,
Bardwell James C. A.,
Saper Mark A.
Publication year - 2000
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/19.4.749
Subject(s) - biology , rna recognition motif , rna , ribosome , structural motif , rna binding protein , ribosomal protein , transfer rna , 5.8s ribosomal rna , sequence motif , ribosomal rna , biochemistry , binding site , microbiology and biotechnology , genetics , dna , gene
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.