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TitleStructural characterization of a eukaryotic chaperone--the ribosome-associated complex.
Journal, issue, pagesNat Struct Mol Biol, Vol. 20, Issue 1, Page 23-28, Year 2013
Publish dateDec 2, 2012
AuthorsChristoph Leidig / Gert Bange / Jürgen Kopp / Stefan Amlacher / Ajay Aravind / Stephan Wickles / Gregor Witte / Ed Hurt / Roland Beckmann / Irmgard Sinning /
PubMed AbstractRibosome-associated chaperones act in early folding events during protein synthesis. Structural information is available for prokaryotic chaperones (such as trigger factor), but structural ...Ribosome-associated chaperones act in early folding events during protein synthesis. Structural information is available for prokaryotic chaperones (such as trigger factor), but structural understanding of these processes in eukaryotes lags far behind. Here we present structural analyses of the eukaryotic ribosome-associated complex (RAC) from Saccharomyces cerevisiae and Chaetomium thermophilum, consisting of heat-shock protein 70 (Hsp70) Ssz1 and the Hsp40 Zuo1. RAC is an elongated complex that crouches over the ribosomal tunnel exit and seems to be stabilized in a distinct conformation by expansion segment ES27. A unique α-helical domain in Zuo1 mediates ribosome interaction of RAC near the ribosomal proteins L22e and L31e and ribosomal RNA helix H59. The crystal structure of the Ssz1 ATPase domain bound to ATP-Mg²⁺ explains its catalytic inactivity and suggests that Ssz1 may act before the RAC-associated chaperone Ssb. Our study offers insights into the interplay between RAC, the ER membrane-integrated Hsp40-type protein ERj1 and the signal-recognition particle.
External linksNat Struct Mol Biol / PubMed:23202586
MethodsEM (single particle) / X-ray diffraction
Resolution1.3 - 9.6 Å
Structure data

EMDB-2179:
Electron cryo-microscopy of C. thermophilum RAC bound to the 80S ribosome
Method: EM (single particle) / Resolution: 9.6 Å

PDB-4gmq:
Ribosome-binding domain of Zuo1
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

PDB-4gni:
Structure of the Ssz1 ATPase bound to ATP and Magnesium
Method: X-RAY DIFFRACTION / Resolution: 1.796 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

Source
  • Chaetomium thermophilum (fungus)
  • chaetomium thermophilum var. thermophilum dsm 1495 (fungus)
Keywordsribosome-binding protein / ribosome binding / co-translational chaperone / CHAPERONE / Hsp70-type ATPase / ATP binding protein / magnesium binding / ribosome-associated complex / RAC

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