期刊
BIOCHEMICAL SOCIETY TRANSACTIONS
卷 44, 期 -, 页码 1561-1569出版社
PORTLAND PRESS LTD
DOI: 10.1042/BST20160190
关键词
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资金
- BBSRC [BB/N014200/1, BB/N005961/1, BB/ J006076/1]
- Leverhulme Trust [RPG-2013-147]
- Human Frontiers Science Program [RGP0014/2014]
- BBSRC [BB/J006076/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/N005961/1, BB/N014200/1, BB/J006076/1] Funding Source: researchfish
The histone-like nucleoid structuring (H-NS) protein is a major component of the folded chromosome in Escherichia coli and related bacteria. Functions attributed to H-NS include management of genome evolution, DNA condensation, and transcription. The wide-ranging influence of H-NS is remarkable given the simplicity of the protein, a small peptide, possessing rudimentary determinants for self-association, hetero-oligomerisation and DNA binding. In this review, I will discuss our understanding of H-NS with a focus on these structural elements. In particular, I will consider how these interaction surfaces allow H-NS to exert its different effects.
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