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An ancestral nuclear protein assembly: crystal structure of the
Methanopyrus kandleri histone.
(PMID:11567091)
* [23]Abstract This article is available in UKPMC
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[28]Fahrner RL,
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[30]Cascio D,
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[32]Lake JA,
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[34]Slesarev A
Department of Chemistry and Biochemistry, University of California, Los
Angeles, California 90095-1570, USA.
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[36]Protein Science : a Publication of the Protein Society [2001,
10(10):2002-7]
Type: Journal Article, Comparative Study
DOI: 10.1110/ps.10901 The Digital Object Identifier (DOI) System
enables identification of digital entities
Abstract Highlight Terms Highlight biological terms.
[ ] Gene Ontology(2) [ ] Species(3)
Eukaryotic histone proteins condense DNA into compact structures called
[37]nucleosomes. [38]Nucleosomes were viewed as a distinguishing
feature of [39]eukaryotes prior to identification of histone orthologs
in methanogens. Although evolutionarily distinct from methanogens, the
methane-producing hyperthermophile [40]Methanopyrus kandleri produces a
novel, 154-residue histone (HMk). Amino acid sequence comparisons show
that HMk differs from both methanogenic and eukaryotic histones, in
that it contains two histone-fold ms within a single chain. The two HMk
histone-fold ms, N and C terminal, are 28% identical in amino acid
sequence to each other and approximately 21% identical in amino acid
sequence to other histone proteins. Here we present the
1.37-A-resolution crystal structure of HMk and report that the HMk
monomer structure is homologous to the eukaryotic histone heterodimers.
In the crystal, HMk forms a dimer homologous to [H3-H4](2) in the
eukaryotic [41]nucleosome. Based on the spatial similarities to
structural ms found in the eukaryotic [42]nucleosome that are important
for [43]DNA-binding, we infer that the [44]Methanopyrus histone binds
DNA in a manner similar to the eukaryotic histone tetramer [H3-H4](2).
[45]Read Article at www.proteinscience.org (Subscription required)
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