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本文引用的文献

1
Structural disorder in amyloid fibrils: its implication in dynamic interactions of proteins.淀粉样纤维中的结构紊乱:其在蛋白质动态相互作用中的意义。
FEBS J. 2009 Oct;276(19):5406-15. doi: 10.1111/j.1742-4658.2009.07250.x. Epub 2009 Aug 27.
2
Attachment of Streptomyces coelicolor is mediated by amyloidal fimbriae that are anchored to the cell surface via cellulose.天蓝色链霉菌的附着是由通过纤维素锚定在细胞表面的淀粉样菌毛介导的。
Mol Microbiol. 2009 Sep;73(6):1128-40. doi: 10.1111/j.1365-2958.2009.06838.x. Epub 2009 Aug 11.
3
Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+].解析酵母朊病毒[PSI+]的感染性结构、菌株变体和物种屏障。
Nat Struct Mol Biol. 2009 Jun;16(6):598-605. doi: 10.1038/nsmb.1617.
4
Soluble amyloid beta-oligomers affect dielectric membrane properties by bilayer insertion and domain formation: implications for cell toxicity.可溶性淀粉样β寡聚体通过双层插入和结构域形成影响介电膜特性:对细胞毒性的影响。
Biophys J. 2008 Nov 15;95(10):4845-61. doi: 10.1529/biophysj.108.130997. Epub 2008 May 30.
5
Chaperone-dependent amyloid assembly protects cells from prion toxicity.伴侣蛋白依赖性淀粉样蛋白组装可保护细胞免受朊病毒毒性的影响。
Proc Natl Acad Sci U S A. 2008 May 20;105(20):7206-11. doi: 10.1073/pnas.0802593105. Epub 2008 May 14.
6
Biofilm development with an emphasis on Bacillus subtilis.以枯草芽孢杆菌为重点的生物膜形成
Curr Top Microbiol Immunol. 2008;322:1-16. doi: 10.1007/978-3-540-75418-3_1.
7
Control of cell fate by the formation of an architecturally complex bacterial community.通过形成结构复杂的细菌群落来控制细胞命运。
Genes Dev. 2008 Apr 1;22(7):945-53. doi: 10.1101/gad.1645008.
8
Polymerizing the fibre between bacteria and host cells: the biogenesis of functional amyloid fibres.细菌与宿主细胞间纤维的聚合:功能性淀粉样纤维的生物合成
Cell Microbiol. 2008 Jul;10(7):1413-20. doi: 10.1111/j.1462-5822.2008.01148.x. Epub 2008 Mar 26.
9
Roles of pgaABCD genes in synthesis, modification, and export of the Escherichia coli biofilm adhesin poly-beta-1,6-N-acetyl-D-glucosamine.pgaABCD基因在大肠杆菌生物膜粘附素聚-β-1,6-N-乙酰-D-葡萄糖胺的合成、修饰及输出中的作用。
J Bacteriol. 2008 May;190(10):3670-80. doi: 10.1128/JB.01920-07. Epub 2008 Mar 21.
10
Amyloid adhesins are abundant in natural biofilms.淀粉样黏附素在天然生物膜中含量丰富。
Environ Microbiol. 2007 Dec;9(12):3077-90. doi: 10.1111/j.1462-2920.2007.01418.x.

淀粉样纤维为枯草芽孢杆菌生物膜提供结构完整性。

Amyloid fibers provide structural integrity to Bacillus subtilis biofilms.

机构信息

Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA.

出版信息

Proc Natl Acad Sci U S A. 2010 Feb 2;107(5):2230-4. doi: 10.1073/pnas.0910560107. Epub 2010 Jan 13.

DOI:10.1073/pnas.0910560107
PMID:20080671
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2836674/
Abstract

Bacillus subtilis forms biofilms whose constituent cells are held together by an extracellular matrix. Previous studies have shown that the protein TasA and an exopolysaccharide are the main components of the matrix. Given the importance of TasA in biofilm formation, we characterized the physicochemical properties of this protein. We report that purified TasA forms fibers of variable length and 10-15 nm in width. Biochemical analyses, in combination with the use of specific dyes and microscopic analyses, indicate that TasA forms amyloid fibers. Consistent with this hypothesis, TasA fibers required harsh treatments (e.g., formic acid) to be depolymerized. When added to a culture of a tasA mutant, purified TasA restored wild-type biofilm morphology, indicating that the purified protein retained biological activity. We propose that TasA forms amyloid fibers that bind cells together in the biofilm.

摘要

枯草芽孢杆菌形成生物膜,其组成细胞由细胞外基质结合在一起。先前的研究表明,TasA 蛋白和一种胞外多糖是基质的主要成分。鉴于 TasA 在生物膜形成中的重要性,我们对该蛋白的物理化学性质进行了表征。我们报告说,纯化的 TasA 形成长度可变且宽度为 10-15nm 的纤维。生化分析结合使用特定的染料和显微镜分析表明,TasA 形成淀粉样纤维。与该假设一致,TasA 纤维需要苛刻的处理(例如甲酸)才能解聚。当添加到 tasA 突变体的培养物中时,纯化的 TasA 恢复了野生型生物膜形态,表明纯化的蛋白保留了生物活性。我们提出 TasA 形成淀粉样纤维,将生物膜中的细胞结合在一起。