The structural organization of the N-terminus domain of SopB, a virulence factor of Salmonella, depends on the nature of its protein partners.

The structural organization of the N-terminus domain of SopB, a virulence factor of Salmonella, depends on the nature of its protein partners.
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SopB(沙门氏菌的毒力因子)的 N 末端结构域的结构组织取决于其蛋白质伙伴的性质。

DOI:
10.1016/j.bbapap.2013.09.014
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发表时间:
2013
期刊:
Biochimica et biophysica acta
影响因子:
--
通讯作者:
C. Bompard
C. Bompard
中科院分区:
--
文献类型:
--
作者:
P. Roblin;Pierre Lebrun;P. Rucktooa;F. Dewitte;Zoé Lens;V. Receveur;V. Raussens;V. Villeret;C. Bompard

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沙门氏菌和许多细菌病原体使用TTSS将毒力因子直接注射到靶真核细胞的细胞质中。一旦转移,这些所谓的效应蛋白质就会劫持大量关键的细胞功能,使细菌受益。在细菌细胞质中,一些效应子通过与特定的III型分子伴侣相互作用而稳定并维持在分泌能力状态。本研究采用生物化学、生物物理和结构分析相结合的方法,对沙门氏菌外蛋白B(Sop B)分子伴侣结合结构域的构象进行了研究。我们的研究结果表明,SopB的N端部分主要由α-螺旋和未折叠区域组成,它们的组织/稳定依赖于它们与不同伙伴的相互作用。这表明,该N-末端区域的部分未折叠状态赋予效应子在感染周期中结合非常不同的伴侣的适应性,允许细菌调节许多宿主细胞功能,限制易位效应子的数量。
The TTSS is used bySalmonellaand many bacterial pathogens to inject virulence factors directly into the cytoplasm of target eukaryotic cells. Once translocated these so-called effector proteins hijack a vast array of crucial cellular functions to the benefit of the bacteria. In the bacterial cytoplasm, some effectors are stabilized and maintained in a secretion competent state by interaction with specific type III chaperones. In this work we studied the conformation of the Chaperone Binding Domain of the effector namedSalmonellaOuter protein B (SopB) alone and in complex with its cognate chaperone SigE by a combination of biochemical, biophysical and structural approaches. Our results show that the N-terminus part of SopB is mainly composed by α-helices and unfolded regions whose organization/stabilization depends on their interaction with the different partners. This suggests that the partially unfolded state of this N-terminal region, which confers the adaptability of the effector to bind very different partners during the infection cycle, allows the bacteria to modulate numerous host cells functions limiting the number of translocated effectors.
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