Structure of histone-based chromatin in Archaea | Zendy

Francesca Mattiroli | Zendy; Sudipta Bhattacharyya | Zendy; Pamela N. Dyer | Zendy; Alison E. White | Zendy; Kathleen Sandman | Zendy; Brett W. Burkhart | Zendy; Kyle R. Byrne | Zendy; Thomas Lee | Zendy; Natalie G. Ahn | Zendy; Thomas J. Santangelo | Zendy; John N. Reeve | Zendy; Karolin Luger | Zendy

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Structure of histone-based chromatin in Archaea

Author(s) -

Francesca Mattiroli,

Sudipta Bhattacharyya,

Pamela N. Dyer,

Alison E. White,

Kathleen Sandman,

Brett W. Burkhart,

Kyle R. Byrne,

Thomas Lee,

Natalie G. Ahn,

Thomas J. Santangelo,

John N. Reeve,

Karolin Luger

Publication year - 2017

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.aaj1849

Subject(s) - nucleosome , chromatin , histone , hyperthermophile , histone code , superhelix , histone octamer , biology , histone h1 , histone h2a , genetics , archaea , microbiology and biotechnology , dna , dna replication , dna supercoil , gene

Small basic proteins present in most Archaea share a common ancestor with the eukaryotic core histones. We report the crystal structure of an archaeal histone-DNA complex. DNA wraps around an extended polymer, formed by archaeal histone homodimers, in a quasi-continuous superhelix with the same geometry as DNA in the eukaryotic nucleosome. Substitutions of a conserved glycine at the interface of adjacent protein layers destabilize archaeal chromatin, reduce growth rate, and impair transcription regulation, confirming the biological importance of the polymeric structure. Our data establish that the histone-based mechanism of DNA compaction predates the nucleosome, illuminating the origin of the nucleosome.

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