期刊
FEBS LETTERS
卷 586, 期 2, 页码 132-136出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2011.12.020
关键词
Bacillus; Growth inhibition; Pfam PF04740; Ribonuclease; RNase; Toxin/antitoxin protein
资金
- National Science Foundation [0642052]
- National Institutes of Health [GM078634]
- Direct For Biological Sciences [0642052] Funding Source: National Science Foundation
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1027546] Funding Source: National Science Foundation
- Div Of Molecular and Cellular Bioscience [0642052] Funding Source: National Science Foundation
The C-terminal regions (CT) of Pfam PF04740 proteins share significant sequence identity with the toxic CdiA-CT effector domains of contact-dependent growth inhibition (CDI) systems. In accord with this homology, we find that several PF04740 CT domains inhibit cell growth when expressed in Escherichia coli. This growth inhibition is specifically blocked by antitoxin proteins encoded downstream of each PF04740 gene. The YobL-CT, YxiD-CT and YqcG-CT domains from Bacillus subtilis 168 have cytotoxic RNase activities, which are neutralized by the binding of cognate YobK, YxxD and YqcF antitoxin proteins, respectively. Our results show that PF04740 proteins represent a new family of toxin/antitoxin pairs that are widely distributed in Gram-positive bacteria. Structured summary of protein interactions: YobK binds to YobL by pull down (View interaction) YezG binds to YeeF by pull down (View interaction) (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据