The Chaperone Network Connected to Human Ribosome-Associated Complex

Author:

Jaiswal Himjyot12,Conz Charlotte13,Otto Hendrik1,Wölfle Tina1,Fitzke Edith1,Mayer Matthias P.4,Rospert Sabine13

Affiliation:

1. Institute of Biochemistry and Molecular Biology, ZBMZ, University of Freiburg, Stefan-Meier-Str. 17, D-79104 Freiburg, Germany

2. Faculty of Biologie, University of Freiburg, Schänzlestr. 1, D-79104 Freiburg, Germany

3. Centre for Biological Signaling Studies (BIOSS), University of Freiburg, Freiburg, Germany

4. Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH-Allianz, D-69120 Heidelberg, Germany

Abstract

ABSTRACT Mammalian ribosome-associated complex (mRAC), consisting of the J-domain protein MPP11 and the atypical Hsp70 homolog (70-homolog) Hsp70L1, can partly complement the function of RAC, which is the homologous complex from Saccharomyces cerevisiae . RAC is the J-domain partner exclusively of the 70-homolog Ssb, which directly and independently of RAC binds to the ribosome. We here show that growth defects due to mRAC depletion in HeLa cells resemble those of yeast strains lacking RAC. Functional conservation, however, did not extend to the 70-homolog partner of mRAC. None of the major human 70-homologs was able to complement the growth defects of yeast strains lacking Ssb or was bound to ribosomes in an Ssb-like manner. Instead, our data suggest that mRAC was a specific partner of human Hsp70 but not of its close homolog Hsc70. On a mechanistic level, ATP binding, but not ATP hydrolysis, by Hsp70L1 affected mRAC's function as a J-domain partner of Hsp70. The combined data indicate that, while functionally conserved, yeast and mammalian cells have evolved distinct solutions to ensure that Hsp70-type chaperones can efficiently assist the biogenesis of newly synthesized polypeptide chains.

Publisher

American Society for Microbiology

Subject

Cell Biology,Molecular Biology

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