The DNA-binding protein HTa from Thermoplasma acidophilum is an archaeal histone analog.

Autor:	Hocher A; MRC London Institute of Medical Sciences (LMS), London, United Kingdom.; Institute of Clinical Sciences (ICS), Faculty of Medicine, Imperial College, London, United Kingdom., Rojec M; MRC London Institute of Medical Sciences (LMS), London, United Kingdom.; Institute of Clinical Sciences (ICS), Faculty of Medicine, Imperial College, London, United Kingdom., Swadling JB; MRC London Institute of Medical Sciences (LMS), London, United Kingdom.; Institute of Clinical Sciences (ICS), Faculty of Medicine, Imperial College, London, United Kingdom., Esin A; MRC London Institute of Medical Sciences (LMS), London, United Kingdom.; Institute of Clinical Sciences (ICS), Faculty of Medicine, Imperial College, London, United Kingdom., Warnecke T; MRC London Institute of Medical Sciences (LMS), London, United Kingdom.; Institute of Clinical Sciences (ICS), Faculty of Medicine, Imperial College, London, United Kingdom.
Jazyk:	angličtina
Zdroj:	ELife [Elife] 2019 Nov 11; Vol. 8. Date of Electronic Publication: 2019 Nov 11.
DOI:	10.7554/eLife.52542
Abstrakt:	Histones are a principal constituent of chromatin in eukaryotes and fundamental to our understanding of eukaryotic gene regulation. In archaea, histones are widespread but not universal: several lineages have lost histone genes. What prompted or facilitated these losses and how archaea without histones organize their chromatin remains largely unknown. Here, we elucidate primary chromatin architecture in an archaeon without histones, Thermoplasma acidophilum, which harbors a HU family protein (HTa) that protects part of the genome from micrococcal nuclease digestion. Charting HTa-based chromatin architecture in vitro, in vivo and in an HTa-expressing E. coli strain, we present evidence that HTa is an archaeal histone analog. HTa preferentially binds to GC-rich sequences, exhibits invariant positioning throughout the growth cycle, and shows archaeal histone-like oligomerization behavior. Our results suggest that HTa, a DNA-binding protein of bacterial origin, has converged onto an architectural role filled by histones in other archaea. Competing Interests: AH, MR, JS, AE, TW No competing interests declared (© 2019, Hocher et al.)
Databáze:	MEDLINE
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