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Proc Natl Acad Sci U S A. 2002 Apr 2;99(7):4209-14.

A functional chaperone triad on the yeast ribosome.

Author information

  • 1Max-Planck Research Unit Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle, Saale, Germany.

Abstract

The chaperones RAC (ribosome-associated complex), consisting of Ssz1p and zuotin, and Ssb1/2p are associated with ribosomes of yeast. Ssb1/2p was previously shown to form a crosslink product to polypeptides trapped in ribosome-nascent chain complexes (RNCs) in vitro. Here we show that an efficient crosslink of the nascent chain to Ssb1/2p depends on the presence of functional RAC. The crosslink to Ssb1/2p was significantly diminished if (i) RAC was removed from RNCs: a process reversed by addition of purified RAC; (ii) RAC carried a mutation in the J-domain of zuotin, leading to its inactivation in vivo; (iii) RAC's Ssz1p subunit was absent because RNCs were generated in a Deltassz1-derived translation extract. In vivo the same specific set of growth defects caused by the absence of any of the three chaperones was also displayed by a Deltassb1/2Deltassz1Deltazuo1 strain. The combination of in vitro and in vivo data supports a model in which Ssb1/2p, Ssz1p, and zuotin act in concert on nascent chains while they are being synthesized.

PMID:
11929994
[PubMed - indexed for MEDLINE]
PMCID:
PMC123627
Free PMC Article

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