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

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Dudek, J, Volkmer, J, Bies, C, Guth, S, Müller, A, Lerner, M, Feick, P, Schäfer, K, Morgenstern, E, Hennessy, F, Blatch, Gregory L, Janoscheck, K, Heim, N, Scholtes, P, Frien, M, 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.

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

Item type Article
URI https://vuir.vu.edu.au/id/eprint/21307
DOI https://doi.org/10.1093/emboj/cdf315
Official URL http://www.nature.com/emboj/journal/v21/n12/full/7...
Subjects Historical > Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
Current > FOR Classification > 0601 Biochemistry and Cell Biology
Keywords BiP, endoplasmic reticulum, molecular chaperones, Mtj1p, ribosome
Citations in Scopus 0 - View on Scopus
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