The ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb.
Crystallography, X-Ray
DNA-Binding Proteins
/ metabolism
HSP40 Heat-Shock Proteins
/ chemistry
HSP70 Heat-Shock Proteins
/ chemistry
Models, Molecular
Molecular Chaperones
/ chemistry
Protein Binding
Protein Folding
Ribosomes
/ metabolism
Saccharomyces cerevisiae
/ metabolism
Saccharomyces cerevisiae Proteins
/ chemistry
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
20 03 2020
20 03 2020
Historique:
received:
17
09
2019
accepted:
03
03
2020
entrez:
22
3
2020
pubmed:
22
3
2020
medline:
18
7
2020
Statut:
epublish
Résumé
The conserved ribosome-associated complex (RAC) consisting of Zuo1 (Hsp40) and Ssz1 (non-canonical Hsp70) acts together with the ribosome-bound Hsp70 chaperone Ssb in de novo protein folding at the ribosomal tunnel exit. Current models suggest that the function of Ssz1 is confined to the support of Zuo1, however, it is not known whether RAC by itself serves as a chaperone for nascent chains. Here we show that, via its rudimentary substrate binding domain (SBD), Ssz1 directly binds to emerging nascent chains prior to Ssb. Structural and biochemical analyses identify a conserved LP-motif at the Zuo1 N-terminus forming a polyproline-II helix, which binds to the Ssz1-SBD as a pseudo-substrate. The LP-motif competes with nascent chain binding to the Ssz1-SBD and modulates nascent chain transfer. The combined data indicate that Ssz1 is an active chaperone optimized for transient, low-affinity substrate binding, which ensures the flux of nascent chains through RAC/Ssb.
Identifiants
pubmed: 32198371
doi: 10.1038/s41467-020-15313-w
pii: 10.1038/s41467-020-15313-w
pmc: PMC7083937
doi:
Substances chimiques
DNA-Binding Proteins
0
HSP40 Heat-Shock Proteins
0
HSP70 Heat-Shock Proteins
0
Molecular Chaperones
0
SSZ1 protein, S cerevisiae
0
Saccharomyces cerevisiae Proteins
0
ZUO1 protein, S cerevisiae
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1504Références
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