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卷曲菌毛的生物合成:通过VIII型分泌途径进行的细菌淀粉样蛋白组装

Curli Biogenesis: Bacterial Amyloid Assembly by the Type VIII Secretion Pathway.

作者信息

Bhoite Sujeet, van Gerven Nani, Chapman Matthew R, Remaut Han

机构信息

Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109.

Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.

出版信息

EcoSal Plus. 2019 Mar;8(2). doi: 10.1128/ecosalplus.ESP-0037-2018.

DOI:10.1128/ecosalplus.ESP-0037-2018
PMID:30892177
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6428212/
Abstract

In 1989, Normark and coworkers reported on fibrous surface structures called curli on strains of that were suspected of causing bovine mastitis. Subsequent work by many groups has revealed an elegant and highly regulated curli biogenesis pathway also referred to as the type VIII secretion system. Curli biogenesis is governed by two divergently transcribed operons, and . The operon encodes the structural subunits of curli, CsgA and CsgB, along with a chaperone-like protein, CsgC. The operon encodes the accessory proteins required for efficient transcription, secretion, and assembly of the curli fiber. CsgA and CsgB are secreted as largely unstructured proteins and transition to β-rich structures that aggregate into regular fibers at the cell surface. Since both of these proteins have been shown to be amyloidogenic in nature, the correct spatiotemporal synthesis of the curli fiber is of paramount importance for proper functioning and viability. Gram-negative bacteria have evolved an elegant machinery for the safe handling, secretion, and extracellular assembly of these amyloidogenic proteins.

摘要

1989年,诺马克及其同事报道了一种名为卷曲菌毛的纤维状表面结构,存在于疑似导致牛乳腺炎的菌株中。随后许多研究小组的工作揭示了一种精巧且高度调控的卷曲菌毛生物合成途径,也被称为VIII型分泌系统。卷曲菌毛的生物合成由两个反向转录的操纵子,即csgBAC和csgDEFG控制。csgBAC操纵子编码卷曲菌毛的结构亚基CsgA和CsgB,以及一种类似伴侣蛋白的CsgC。csgDEFG操纵子编码卷曲菌毛纤维高效转录、分泌和组装所需的辅助蛋白。CsgA和CsgB以基本上无结构的蛋白质形式分泌,并转变为富含β折叠的结构,在细胞表面聚集成规则的纤维。由于这两种蛋白质在本质上都已被证明具有淀粉样变性,卷曲菌毛纤维正确的时空合成对于其正常功能和生存能力至关重要。革兰氏阴性菌已经进化出一种精巧的机制,用于安全处理、分泌和在细胞外组装这些淀粉样变性蛋白质。

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本文引用的文献

1
Structure-Function Analysis of the Curli Accessory Protein CsgE Defines Surfaces Essential for Coordinating Amyloid Fiber Formation.卷曲相关附属蛋白 CsgE 的结构-功能分析定义了协调淀粉样纤维形成所必需的表面。
mBio. 2018 Jul 17;9(4):e01349-18. doi: 10.1128/mBio.01349-18.
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The Role of Functional Amyloids in Bacterial Virulence.功能性淀粉样蛋白在细菌毒力中的作用。
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The FapF Amyloid Secretion Transporter Possesses an Atypical Asymmetric Coiled Coil.FapF 淀粉样蛋白分泌转运蛋白具有非典型的不对称卷曲螺旋。
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Structural and functional characterization of the Curli adaptor protein CsgF.卷曲菌毛衔接蛋白 CsgF 的结构与功能表征。
FEBS Lett. 2018 Mar;592(6):1020-1029. doi: 10.1002/1873-3468.13002. Epub 2018 Feb 21.
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Nucleation and growth of a bacterial functional amyloid at single-fiber resolution.细菌功能性淀粉样蛋白在单纤维分辨率下的成核与生长
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Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade.蛋白质错误折叠、淀粉样纤维形成与人类疾病:过去十年研究进展综述。
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Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation.CsgE的溶液核磁共振结构:对功能性淀粉样蛋白形成起重要作用的伴侣和调节蛋白的结构见解
Proc Natl Acad Sci U S A. 2016 Jun 28;113(26):7130-5. doi: 10.1073/pnas.1607222113. Epub 2016 Jun 13.
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Intrinsic aggregation propensity of the CsgB nucleator protein is crucial for curli fiber formation.CsgB成核蛋白的内在聚集倾向对卷曲纤维的形成至关重要。
J Struct Biol. 2016 Aug;195(2):179-189. doi: 10.1016/j.jsb.2016.05.012. Epub 2016 May 28.
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Electrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperones.CsgC样伴侣蛋白家族对卷曲菌毛淀粉样蛋白成核的静电引导抑制作用。
Sci Rep. 2016 Apr 21;6:24656. doi: 10.1038/srep24656.
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Bacterial amyloid formation: structural insights into curli biogensis.细菌淀粉样蛋白的形成:卷曲菌毛生物合成的结构见解
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