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RbmA 的结构动力学控制生物膜的可塑性。

Structural dynamics of RbmA governs plasticity of biofilms.

机构信息

Department of Microbiology and Environmental Toxicology, University of California, Santa Cruz, Santa Cruz, United States.

Department of Chemistry and Biochemistry, University of California, Santa Cruz, Santa Cruz, United States.

出版信息

Elife. 2017 Aug 1;6:e26163. doi: 10.7554/eLife.26163.

DOI:10.7554/eLife.26163
PMID:28762945
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5605196/
Abstract

Biofilm formation is critical for the infection cycle of exopolysaccharides (VPS) and the matrix proteins RbmA, Bap1 and RbmC are required for the development of biofilm architecture. We demonstrate that RbmA binds VPS directly and uses a binary structural switch within its first fibronectin type III (FnIII-1) domain to control RbmA structural dynamics and the formation of VPS-dependent higher-order structures. The structural switch in FnIII-1 regulates interactions in trans with the FnIII-2 domain, leading to open (monomeric) or closed (dimeric) interfaces. The ability of RbmA to switch between open and closed states is important for biofilm formation, as RbmA variants with switches that are locked in either of the two states lead to biofilms with altered architecture and structural integrity.

摘要

生物膜的形成对于胞外多糖 (VPS) 的感染周期至关重要，而基质蛋白 RbmA、Bap1 和 RbmC 则是生物膜结构发育所必需的。我们证明了 RbmA 可以直接结合 VPS，并在其第一个纤连蛋白 III 型 (FnIII-1) 结构域内使用二元结构开关来控制 RbmA 的结构动力学和 VPS 依赖性高级结构的形成。FnIII-1 结构开关调节与 FnIII-2 结构域的反式相互作用，导致开放（单体）或关闭（二聚体）界面。RbmA 在开放和关闭状态之间切换的能力对于生物膜的形成很重要，因为处于这两种状态之一的开关锁定的 RbmA 变体导致生物膜的结构和结构完整性发生改变。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb0a/5605196/c2594226de00/elife-26163-fig7.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb0a/5605196/c2594226de00/elife-26163-fig7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb0a/5605196/c609f734a2c1/elife-26163-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb0a/5605196/43bcef67c48e/elife-26163-fig1-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb0a/5605196/8b2cf9255a95/elife-26163-fig1-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb0a/5605196/3c091ca0e201/elife-26163-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb0a/5605196/672ad3b59646/elife-26163-fig2-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb0a/5605196/01d5f076c910/elife-26163-fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb0a/5605196/8bd365fd9c01/elife-26163-fig3-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb0a/5605196/49c849535b07/elife-26163-fig3-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb0a/5605196/044aa7b4e6c2/elife-26163-fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb0a/5605196/39342c8e64e2/elife-26163-fig4-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb0a/5605196/b7ada563b156/elife-26163-fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb0a/5605196/d54d3797a176/elife-26163-fig5-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb0a/5605196/0d6c184bf42b/elife-26163-fig6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb0a/5605196/57a8bf83e281/elife-26163-fig6-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb0a/5605196/dafd5900ed17/elife-26163-fig6-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb0a/5605196/97faafd27d6c/elife-26163-fig6-figsupp3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eb0a/5605196/c2594226de00/elife-26163-fig7.jpg

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