期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 431, 期 4, 页码 653-672出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2019.01.001
关键词
HU; bacterial chromatin protein; tethered particle motion; fluorescence microscopy; electrophoretic mobility shift assay
资金
- Vidi Fellowship from the Netherlands Organization for Scientific Research (NWO) [864.10.003]
- Gisela Their Fellowship from the Leiden University Medical Center
- Netherlands Organization for Scientific Research (NWO) [Vici 016.160.613]
- Human Frontier Science Program [RGP0014/2014]
- China Scholarship Council [201506880001]
The maintenance and organization of the chromosome plays an important role in the development and survival of bacteria. Bacterial chromatin proteins are architectural proteins that bind DNA and modulate its conformation, and by doing so affect a variety of cellular processes. No bacterial chromatin proteins of Clostridium difficile have been characterized to date. Here, we investigate aspects of the C. difficile HupA protein, a homologue of the histone-like HU proteins of Escherichia coll. HupA is a 10-kDa protein that is present as a homodimer in vitro and self-interacts in vivo. HupA co-localizes with the nucleoid of C. difficile. It binds to the DNA without a preference for the DNA G + C content. Upon DNA binding, HupA induces a conformational change in the substrate DNA in vitro and leads to compaction of the chromosome in vivo. The present study is the first to characterize a bacterial chromatin protein in C. difficile and opens the way to study the role of chromosomal organization in DNA metabolism and on other cellular processes in this organism. (C) 2019 The Authors. Published by Elsevier Ltd.
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