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A novel type of co-chaperone mediates transmembrane recruitment of DnaK-like chaperones to ribosomes

Dudek, J and Volkmer, J and Bies, C and Guth, S and Müller, A and Lerner, M and Feick, P and Schäfer, K and Morgenstern, E and Hennessy, F and Blatch, Gregory L and Janoscheck, K and Heim, N and Scholtes, P and Frien, M and Nastainczyk, W and Zimmermann, R (2002) A novel type of co-chaperone mediates transmembrane recruitment of DnaK-like chaperones to ribosomes. EMBO Journal, 21 (12). pp. 2958-2967. ISSN 0261-4189

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Abstract

Recently, the homolog of yeast protein Sec63p was identified in dog pancreas microsomes. This pancreatic DnaJ-like protein was shown to be an abundant protein, interacting with both the Sec61p complex and lumenal DnaK-like proteins, such as BiP. The pancreatic endoplasmic reticulum contains a second DnaJ-like membrane protein, which had been termed Mtj1p in mouse. Mtj1p is present in pancreatic microsomes at a lower concentration than Sec63p but has a higher affinity for BiP. In addition to a lumenal J-domain, Mtj1p contains a single transmembrane domain and a cytosolic domain which is in close contact with translating ribosomes and appears to have the ability to modulate translation. The interaction with ribosomes involves a highly charged region within the cytosolic domain of Mtj1p. We propose that Mtj1p represents a novel type of co-chaperone, mediating transmembrane recruitment of DnaK-like chaperones to ribosomes and, possibly, transmembrane signaling between ribosomes and DnaK-like chaperones of the endoplasmic reticulum.

Item Type: Article
Additional Information:

Corrigendum for this article was published the The EMBO journal, 21:14, p. 3917

Uncontrolled Keywords: BiP, endoplasmic reticulum, molecular chaperones, Mtj1p, ribosome
Subjects: Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
FOR Classification > 0601 Biochemistry and Cell Biology
Depositing User: Ms Lyn Wade
Date Deposited: 09 Oct 2012 05:32
Last Modified: 23 Dec 2014 22:39
URI: http://vuir.vu.edu.au/id/eprint/21307
DOI: 10.1093/emboj/cdf315
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Citations in Scopus: 0 - View on Scopus

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