Dudek, J, Volkmer, J, Bies, C, Guth, S, Müller, A, Lerner, M, Feick, P, Schäfer, K, Morgenstern, E, Hennessy, F, Blatch, Gregory ORCID: 0000-0003-0778-8577, 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

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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• A novel type of co-chaperone mediates transmembrane recruitment of DnaK-like chaperones to ribosomes : corrigendum. (deposited 09 Oct 2012 05:30)
  • A novel type of co-chaperone mediates transmembrane recruitment of DnaK-like chaperones to ribosomes. (deposited 09 Oct 2012 05:32) [Currently Displayed]

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