PT  - JOURNAL ARTICLE
AU  - Ana M. Oliveira Paiva
AU  - Annemieke H. Friggen
AU  - Liang Qin
AU  - Roxanne Douwes
AU  - Remus T. Dame
AU  - Wiep Klaas Smits
TI  - The bacterial chromatin protein HupA can remodel DNA and associates with the nucleoid in <em>Clostridium difficile</em>
AID  - 10.1101/426809
DP  - 2018 Jan 01
TA  - bioRxiv
PG  - 426809
4099  - http://biorxiv.org/content/early/2018/12/20/426809.short
4100  - http://biorxiv.org/content/early/2018/12/20/426809.full
AB  - 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, modulate its conformation and by doing so affect a variety of cellular processes. No bacterial chromatin proteins of C. 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.