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两个伴侣蛋白相拥：核糖体相关复合物 RAC 的结构与功能。

Two chaperones locked in an embrace: structure and function of the ribosome-associated complex RAC.

机构信息

Institute of Biochemistry and Molecular Biology, ZBMZ, Medical Faculty, University of Freiburg, Freiburg, Germany.

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

出版信息

Nat Struct Mol Biol. 2017 Aug 3;24(8):611-619. doi: 10.1038/nsmb.3435.

DOI:10.1038/nsmb.3435
PMID:28771464
Abstract

Chaperones, which assist protein folding are essential components of every living cell. The yeast ribosome-associated complex (RAC) is a chaperone that is highly conserved in eukaryotic cells. The RAC consists of the J protein Zuo1 and the unconventional Hsp70 homolog Ssz1. The RAC heterodimer stimulates the ATPase activity of the ribosome-bound Hsp70 homolog Ssb, which interacts with nascent polypeptide chains to facilitate de novo protein folding. In addition, the RAC-Ssb system is required to maintain the fidelity of protein translation. Recent work reveals important details of the unique structures of RAC and Ssb and identifies how the chaperones interact with the ribosome. The new findings start to uncover how the exceptional chaperone triad cooperates in protein folding and maintenance of translational fidelity and its connection to extraribosomal functions.

摘要

伴侣蛋白是协助蛋白质折叠的重要组成部分，是每个活细胞的基本组件。酵母核糖体相关复合物（RAC）是伴侣蛋白，在真核细胞中高度保守。RAC 由 J 蛋白 Zuo1 和非典型的 Hsp70 同源物 Ssz1 组成。RAC 异二聚体刺激与新生多肽链相互作用以促进从头折叠的核糖体结合 Hsp70 同源物 Ssb 的 ATP 酶活性。此外，RAC-Ssb 系统对于维持蛋白质翻译的保真度是必需的。最近的工作揭示了 RAC 和 Ssb 独特结构的重要细节，并确定了伴侣蛋白如何与核糖体相互作用。新的发现开始揭示这个特殊的伴侣蛋白三聚体如何在蛋白质折叠和维持翻译保真度以及与核糖体外功能的连接中合作。

相似文献

[1]
Two chaperones locked in an embrace: structure and function of the ribosome-associated complex RAC.

Nat Struct Mol Biol. 2017-8-3

[2]
The ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb.

Nat Commun. 2020-3-20

[3]
Structural inventory of cotranslational protein folding by the eukaryotic RAC complex.

Nat Struct Mol Biol. 2023-5

[4]
Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding.

Nat Commun. 2022-6-14

[5]
Structural insights into a unique Hsp70-Hsp40 interaction in the eukaryotic ribosome-associated complex.

Nat Struct Mol Biol. 2017-1-9

[6]
The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1.

Nat Struct Mol Biol. 2005-6

[7]
The in vivo function of the ribosome-associated Hsp70, Ssz1, does not require its putative peptide-binding domain.

Proc Natl Acad Sci U S A. 2002-4-2

[8]
Pathway of Hsp70 interactions at the ribosome.

Nat Commun. 2021-9-27

[9]
Structural characterization of a eukaryotic chaperone--the ribosome-associated complex.

Nat Struct Mol Biol. 2012-12-2

[10]
Functional characterization of the atypical Hsp70 subunit of yeast ribosome-associated complex.

J Biol Chem. 2007-11-23

引用本文的文献

[1]
Anti-Prion Systems in Saccharomyces cerevisiae.

J Neurochem. 2025-3

[2]
Mechanistic Insights into Protein Biogenesis and Maturation on the Ribosome.

J Mol Biol. 2025-2-28

[3]
The yeast 14-3-3 proteins Bmh1 and Bmh2 regulate key signaling pathways.

Front Mol Biosci. 2024-1-24

[4]
NAC and Zuotin/Hsp70 chaperone systems coexist at the ribosome tunnel exit in vivo.

Nucleic Acids Res. 2024-4-12

[5]
Exploration of the truncated cytosolic Hsp70 in plants - unveiling the diverse T1 lineage and the conserved T2 lineage.

Front Plant Sci. 2023-11-16

[6]
The ribosome-associated chaperone Zuo1 controls translation upon TORC1 inhibition.

EMBO J. 2023-12-11

[7]
Structural inventory of cotranslational protein folding by the eukaryotic RAC complex.

Nat Struct Mol Biol. 2023-5

[8]
Interaction of client-the scaffold on which FeS clusters are build-with J-domain protein Hsc20 and its evolving Hsp70 partners.

Front Mol Biosci. 2022-10-12

[9]
Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding.

Nat Commun. 2022-6-14

[10]
Ribosomal protein eL39 is important for maturation of the nascent polypeptide exit tunnel and proper protein folding during translation.

Nucleic Acids Res. 2022-6-24

本文引用的文献

[1]
Structural insights into a unique Hsp70-Hsp40 interaction in the eukaryotic ribosome-associated complex.

Nat Struct Mol Biol. 2017-1-9

[2]
Moonlighting chaperone-like activity of the universal regulatory 14-3-3 proteins.

FEBS J. 2017-1-6

[3]
Multivalent contacts of the Hsp70 Ssb contribute to its architecture on ribosomes and nascent chain interaction.

Nat Commun. 2016-12-5

[4]
Interaction of the cotranslational Hsp70 Ssb with ribosomal proteins and rRNA depends on its lid domain.

Nat Commun. 2016-11-24

[5]
Alternative modes of client binding enable functional plasticity of Hsp70.

Nature. 2016-10-26

[6]
Molecular biology: Mature proteins braced by a chaperone.

Nature. 2016-11-17

[7]
Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits.

Nat Struct Mol Biol. 2016-11

[8]
On-site remodeling at chromatin: How multiprotein complexes are rebuilt during DNA repair and transcriptional activation.

Bioessays. 2016-11

[9]
Silencing of ZRF1 impedes survival of estrogen receptor positive MCF-7 cells and potentiates the effect of curcumin.

Tumour Biol. 2016-9

[10]
The yeast Hsp70 homolog Ssb: a chaperone for general de novo protein folding and a nanny for specific intrinsically disordered protein domains.

Curr Genet. 2017-2

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