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J Mol Biol. 2019 Feb 15;431(4):653-672. doi: 10.1016/j.jmb.2019.01.001. Epub 2019 Jan 8.

The Bacterial Chromatin Protein HupA Can Remodel DNA and Associates with the Nucleoid in Clostridium difficile.

Author information

1
Department of Medical Microbiology, Section Experimental Bacteriology, Leiden University Medical Center, Leiden, the Netherlands; Center for Microbial Cell Biology, Leiden, the Netherlands.
2
Faculty of Science, Leiden Institute of Chemistry, Leiden University, Leiden, the Netherlands; Center for Microbial Cell Biology, Leiden, the Netherlands.
3
Department of Medical Microbiology, Section Experimental Bacteriology, Leiden University Medical Center, Leiden, the Netherlands.
4
Department of Medical Microbiology, Section Experimental Bacteriology, Leiden University Medical Center, Leiden, the Netherlands; Center for Microbial Cell Biology, Leiden, the Netherlands. Electronic address: w.k.smits@lumc.nl.

Abstract

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 coli. 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.

KEYWORDS:

HU; bacterial chromatin protein; electrophoretic mobility shift assay; fluorescence microscopy; tethered particle motion

PMID:
30633871
DOI:
10.1016/j.jmb.2019.01.001
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