Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits

Lee, Kanghyun; Sharma, Ruchika; Shrestha, Om Kumar; Bingman, Craig A.; Craig, Elizabeth A.

doi:10.1038/nsmb.3299

Title: Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits

Journal Article · Mon Sep 26 00:00:00 EDT 2016 · Nature Structural & Molecular Biology

DOI:https://doi.org/10.1038/nsmb.3299· OSTI ID:1357642

Lee, Kanghyun ^[1]; Sharma, Ruchika ^[1]; Shrestha, Om Kumar ^[1]; Bingman, Craig A. ^[1]; Craig, Elizabeth A. ^[1]

Univ. of Wisconsin, Madison, WI (United States)

Ribosome-associated J protein–Hsp70 chaperones promote nascent-polypeptide folding and normal translational fidelity. The J protein Zuo1 is known to span the ribosomal subunits, but understanding of its function is limited. Here, in this paper, we present new structural and cross-linking data allowing more precise positioning of Saccharomyces cerevisiae Zuo1 near the 60S polypeptide-exit site and suggesting interactions of Zuo1 with the ribosomal protein eL31 and 25S rRNA helix 24. The junction between the 60S-interacting and subunit-spanning helices is a hinge that positions Zuo1 on the 40S yet accommodates subunit rotation. Interaction between the Zuo1 C terminus and 40S occurs via 18S rRNA expansion segment 12 (ES12) of helix 44, which originates at the decoding site. Deletions in either ES12 or the Zuo1 C terminus alter readthrough of stop codons and –1 frameshifting. Our study offers insight into how this cotranslational chaperone system may monitor decoding-site activity and nascent-polypeptide transit, thereby coordinating protein translation and folding.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: National Institutes of Health (NIH); USDOE Office of Science (SC); National Cancer Institute (NCI); National Institute of General Medical Sciences (NIGMS)

Grant/Contract Number:: GM031107; GM027870; GM094584; GM094622; GM098248; AC02-06CH11357; ACB-12002; AGM-12006

OSTI ID:: 1357642

Journal Information:: Nature Structural & Molecular Biology, Vol. 23, Issue 11; ISSN 1545-9993

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 29 works

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