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  • The EMBO Journal (2000) 19, 749 - 757
  • doi:10.1093/emboj/19.4.749

Structure of Hsp15 reveals a novel RNA-binding motif

Bart L. Staker1,2, Philipp Korber3, James C. A. Bardwell2,3 and Mark A. Saper1,2

  1. Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA
  2. Biophysics Research Division, University of Michigan, Ann Arbor, MI 48109, USA
  3. Department of Biology, University of Michigan, Ann Arbor, MI 48109, USA

Correspondence to:

James C. A. Bardwell, E-mail: jbardwel@umich.edu

Mark A. Saper, E-mail: saper@umich.edu

Received 31 August 1999; Accepted 20 December 1999; Revised 20 December 1999

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.

  • Keywords:

    • heat shock proteins,
    • protein–RNA interactions,
    • protein structure,
    • ribosome,
    • X-ray crystallography