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本文引用的文献

1
Bacterial and Yeast AAA+ Disaggregases ClpB and Hsp104 Operate through Conserved Mechanism Involving Cooperation with Hsp70.细菌和酵母的AAA+解聚酶ClpB和Hsp104通过与Hsp70协同作用的保守机制发挥作用。
J Mol Biol. 2016 Oct 23;428(21):4378-4391. doi: 10.1016/j.jmb.2016.09.003. Epub 2016 Sep 9.
2
Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation.热休克蛋白104解聚酶的螺旋结构揭示了多肽转运的基础。
Nat Struct Mol Biol. 2016 Sep;23(9):830-7. doi: 10.1038/nsmb.3277. Epub 2016 Aug 1.
3
Adenosine diphosphate restricts the protein remodeling activity of the Hsp104 chaperone to Hsp70 assisted disaggregation.二磷酸腺苷将Hsp104伴侣蛋白的蛋白质重塑活性限制在Hsp70辅助的解聚作用中。
Elife. 2016 May 25;5:e15159. doi: 10.7554/eLife.15159.
4
Mechanistic Insights into Hsp104 Potentiation.Hsp104增强作用的机制性见解。
J Biol Chem. 2016 Mar 4;291(10):5101-15. doi: 10.1074/jbc.M115.707976. Epub 2016 Jan 8.
5
ClpB N-terminal domain plays a regulatory role in protein disaggregation.ClpB蛋白的N端结构域在蛋白质解聚过程中发挥调控作用。
Proc Natl Acad Sci U S A. 2015 Dec 15;112(50):E6872-81. doi: 10.1073/pnas.1512783112. Epub 2015 Nov 30.
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Engineering enhanced protein disaggregases for neurodegenerative disease.设计用于神经退行性疾病的增强型蛋白质解聚酶
Prion. 2015;9(2):90-109. doi: 10.1080/19336896.2015.1020277.
7
The Hsp104 N-terminal domain enables disaggregase plasticity and potentiation.热休克蛋白104（Hsp104）的N端结构域赋予解聚酶可塑性和增强作用。
Mol Cell. 2015 Mar 5;57(5):836-849. doi: 10.1016/j.molcel.2014.12.021. Epub 2015 Jan 22.
8
Deciphering key features in protein structures with the new ENDscript server.利用新的 ENDscript 服务器破译蛋白质结构中的关键特征。
Nucleic Acids Res. 2014 Jul;42(Web Server issue):W320-4. doi: 10.1093/nar/gku316. Epub 2014 Apr 21.
9
Hsp104 overexpression cures Saccharomyces cerevisiae [PSI+] by causing dissolution of the prion seeds.热休克蛋白104（Hsp104）的过表达通过引起朊病毒种子的溶解来治愈酿酒酵母的[PSI+]状态。
Eukaryot Cell. 2014 May;13(5):635-47. doi: 10.1128/EC.00300-13. Epub 2014 Mar 14.
10
Potentiated Hsp104 variants antagonize diverse proteotoxic misfolding events.增强型 Hsp104 变体拮抗多种蛋白毒性错误折叠事件。
Cell. 2014 Jan 16;156(1-2):170-82. doi: 10.1016/j.cell.2013.11.047.

酿酒酵母和白色念珠菌的 Hsp104 N 端结构域的晶体结构表明 Hsp104 在朊病毒溶解中的功能机制。

Crystal structures of Hsp104 N-terminal domains from Saccharomyces cerevisiae and Candida albicans suggest the mechanism for the function of Hsp104 in dissolving prions.

机构信息

Department of Cell, Developmental and Integrative Biology (CDIB), University of Alabama at Birmingham, Birmingham, AL 35294, USA.

Department of Chemistry, University of Alabama at Birmingham, Birmingham, AL 35294, USA.

出版信息

Acta Crystallogr D Struct Biol. 2017 Apr 1;73(Pt 4):365-372. doi: 10.1107/S2059798317002662. Epub 2017 Mar 31.

DOI:10.1107/S2059798317002662
PMID:28375147
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6688567/
Abstract

Hsp104 is a yeast member of the Hsp100 family which functions as a molecular chaperone to disaggregate misfolded polypeptides. To understand the mechanism by which the Hsp104 N-terminal domain (NTD) interacts with its peptide substrates, crystal structures of the Hsp104 NTDs from Saccharomyces cerevisiae (ScHsp104NTD) and Candida albicans (CaHsp104NTD) have been determined at high resolution. The structures of ScHsp104NTD and CaHsp104NTD reveal that the yeast Hsp104 NTD may utilize a conserved putative peptide-binding groove to interact with misfolded polypeptides. In the crystal structures ScHsp104NTD forms a homodimer, while CaHsp104NTD exists as a monomer. The consecutive residues Gln105, Gln106 and Lys107, and Lys141 around the putative peptide-binding groove mediate the monomer-monomer interactions within the ScHsp104NTD homodimer. Dimer formation by ScHsp104NTD suggests that the Hsp104 NTD may specifically interact with polyQ regions of prion-prone proteins. The data may reveal the mechanism by which Hsp104 NTD functions to suppress and/or dissolve prions.

摘要

Hsp104 是酵母细胞中 Hsp100 家族的成员，作为分子伴侣发挥作用，可以使错误折叠的多肽解聚。为了了解 Hsp104 N 端结构域（NTD）与肽底物相互作用的机制，已解析了酿酒酵母（ScHsp104NTD）和白色念珠菌（CaHsp104NTD）的 Hsp104 NTD 的高分辨率晶体结构。ScHsp104NTD 和 CaHsp104NTD 的结构表明，酵母 Hsp104 NTD 可能利用保守的假定肽结合槽与错误折叠的多肽相互作用。在晶体结构中，ScHsp104NTD 形成同源二聚体，而 CaHsp104NTD 则以单体形式存在。假定的肽结合槽周围的连续残基 Gln105、Gln106 和 Lys107 以及 Lys141 介导了 ScHsp104NTD 同源二聚体中的单体-单体相互作用。ScHsp104NTD 的二聚体形成表明 Hsp104 NTD 可能特异性地与朊病毒倾向蛋白的 polyQ 区域相互作用。这些数据可能揭示了 Hsp104 NTD 抑制和/或溶解朊病毒的机制。