Structural basis for interaction of a cotranslational chaperone with the eukaryotic ribosome. (Q43495307)

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22 February 2020

title

Structural basis for interaction of a cotranslational chaperone with the eukaryotic ribosome (English)

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22 February 2020

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10

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Ningning Li

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22 February 2020

author name string

Yixiao Zhang

1

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22 February 2020

Chengying Ma

2

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Yi Yuan

3

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22 February 2020

Jing Zhu

4

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22 February 2020

Chu Chen

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22 February 2020

Shan Wu

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22 February 2020

Li Yu

8

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Jianlin Lei

9

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publication date

2 November 2014

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Nature Structural & Molecular Biology

22 February 2020

published in

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volume

21

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issue

12

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page(s)

1042-1046

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https://scigraph.springernature.com/pub.10.1038/nsmb.2908

22 February 2020

exact match

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cites work

Converging concepts of protein folding in vitro and in vivo

1 reference

The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins

21 January 2018

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Ribosome-associated chaperones as key players in proteostasis

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Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous

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The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex

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A functional chaperone triad on the yeast ribosome

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RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin.

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Zuotin, a ribosome-associated DnaJ molecular chaperone

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The translation machinery and 70 kd heat shock protein cooperate in protein synthesis

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The in vivo function of the ribosome-associated Hsp70, Ssz1, does not require its putative peptide-binding domain

21 January 2018

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The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1.

21 January 2018

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The HSP70 chaperone machinery: J proteins as drivers of functional specificity

21 January 2018

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The ribosome as a hub for protein quality control

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The cotranslational function of ribosome-associated Hsp70 in eukaryotic protein homeostasis

21 January 2018

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Ribosome-associated complex and Ssb are required for translational repression induced by polylysine segments within nascent chains

21 January 2018

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The ribosome-bound chaperones RAC and Ssb1/2p are required for accurate translation in Saccharomyces cerevisiae

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Cotranslational response to proteotoxic stress by elongation pausing of ribosomes

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A dual function for chaperones SSB-RAC and the NAC nascent polypeptide-associated complex on ribosomes

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A ribosome-anchored chaperone network that facilitates eukaryotic ribosome biogenesis

21 January 2018

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Unfolding of the C-Terminal Domain of the J-Protein Zuo1 Releases Autoinhibition and Activates Pdr1-Dependent Transcription

21 January 2018

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Role for the molecular chaperones Zuo1 and Ssz1 in quorum sensing via activation of the transcription factor Pdr1

21 January 2018

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Structural characterization of a eukaryotic chaperone--the ribosome-associated complex

21 January 2018

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The structure of the eukaryotic ribosome at 3.0 Å resolution

21 January 2018

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Ribosome-associated complex binds to ribosomes in close proximity of Rpl31 at the exit of the polypeptide tunnel in yeast

21 January 2018

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A ratchet-like inter-subunit reorganization of the ribosome during translocation

21 January 2018

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The process of mRNA-tRNA translocation

21 January 2018

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Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation

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Structure of the signal recognition particle interacting with the elongation-arrested ribosome.

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21 January 2018

Identifiers

DOI

10.1038/NSMB.2908

1 reference

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22 February 2020

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