This is the authors' abstract. We don't add key points for this paper.
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.
Answers are grounded in this paper and cite their sources.
No takes yet. Share an insight, caveat, or question.
David C. Grainger (2016) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: