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News and Views
Nature Structural Biology  9, 716 - 718 (2002)
doi:10.1038/nsb1002-716

Where chaperones and nascent polypeptides meet

Véronique Albanèse & Judith Frydman

Véronique Albanèse and Judith Frydman are in the Department of Biological Sciences, Stanford University, Stanford, California 94305-5020 USA. jfrydman@stanford.edu

Two recent studies provide evidence for a direct interaction between the ribosomal protein L23 at the exit tunnel of the ribosome and the bacterial chaperone trigger factor, and between the eukaryotic L23 homolog and the signal recognition particle. These findings indicate that the exit site of the ribosome may physically link translation to the cytosolic components that guide nascent polypeptides to their correct fate.

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REFERENCE
Protein Folding In Vivo
Nature Encyclopaedia of Life Sciences
 See all 2 matches for Reference

NEWS AND VIEWS
GTPase twins in the SRP family
Nature Structural & Molecular Biology News and Views (01 Feb 2004)

RESEARCH
MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin
The EMBO Journal Article (01 Dec 1999)
Structure of the signal recognition particle interacting with the elongation-arrested ribosome
Nature Article (26 Feb 2004)
L23 protein functions as a chaperone docking site on the ribosome
Nature Letters to Editor (12 Sep 2002)

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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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