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分枝杆菌严格反应蛋白 Rel 的 C 末端保守无规则区的证据。

Evidence of a conserved intrinsically disordered region in the C-terminus of the stringent response protein Rel from mycobacteria.

机构信息

Microbiology and Molecular Biology Laboratory, Department of Biological Sciences, Indian Institute of Science Education and Research (IISER), Bhopal 462023, India.

Biomolecular Modeling and Design Division, Bioinformatics Institute, A(*)STAR, Singapore 138671, Singapore.

出版信息

FEBS Lett. 2014 May 2;588(9):1839-49. doi: 10.1016/j.febslet.2014.03.048. Epub 2014 Apr 6.

DOI:10.1016/j.febslet.2014.03.048
PMID:24717772
Abstract

The RelA/SpoT enzyme produces (p)ppGpp that helps the bacterium survive during stress. The domains present in it are interspersed with connecting linkers whose functions have been poorly elucidated. We rationally analyzed the sequence and structural property of the regulatory C-terminal region in the Rel family of proteins and report the presence of an intrinsically disordered region between two successive domains in this region that are separated by a defined amino acid sequence length. We show that the length and secondary structure of this linker are conserved in Rel proteins, further signifying its importance in rendering flexibility for domain movement and domain-domain interaction.

摘要

RelA/SpoT 酶产生 (p)ppGpp,帮助细菌在压力下存活。它所包含的结构域与连接接头交错,但其功能尚未得到充分阐明。我们对 Rel 家族蛋白的调控 C 末端区域的序列和结构特性进行了合理分析,并报告了在该区域的两个连续结构域之间存在一个固有无序区域,它们被特定的氨基酸序列长度隔开。我们表明,该接头的长度和二级结构在 Rel 蛋白中是保守的,这进一步表明它在赋予结构域运动和结构域-结构域相互作用的灵活性方面的重要性。

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