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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2001-10-30
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pubmed:abstractText |
The efficient assembly of histone complexes and nucleosomes requires the participation of molecular chaperones. Currently, there is a paucity of data on their mechanism of action. We now present the structure of an N-terminal domain of nucleoplasmin (Np-core) at 2.3 A resolution. The Np-core monomer is an eight-stranded beta barrel that fits snugly within a stable pentamer. In the crystal, two pentamers associate to form a decamer. We show that both Np and Np-core are competent to assemble large complexes that contain the four core histones. Further experiments and modeling suggest that these complexes each contain five histone octamers which dock to a central Np decamer. This work has important ramifications for models of histone storage, sperm chromatin decondensation, and nucleosome assembly.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
841-53
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11684019-Amino Acid Sequence,
pubmed-meshheading:11684019-Animals,
pubmed-meshheading:11684019-Crystallography, X-Ray,
pubmed-meshheading:11684019-Histones,
pubmed-meshheading:11684019-Macromolecular Substances,
pubmed-meshheading:11684019-Models, Molecular,
pubmed-meshheading:11684019-Molecular Sequence Data,
pubmed-meshheading:11684019-Nuclear Proteins,
pubmed-meshheading:11684019-Nucleoplasmins,
pubmed-meshheading:11684019-Nucleosomes,
pubmed-meshheading:11684019-Phosphoproteins,
pubmed-meshheading:11684019-Protein Binding,
pubmed-meshheading:11684019-Protein Folding,
pubmed-meshheading:11684019-Protein Structure, Tertiary,
pubmed-meshheading:11684019-Sequence Alignment
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pubmed:year |
2001
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pubmed:articleTitle |
The crystal structure of nucleoplasmin-core: implications for histone binding and nucleosome assembly.
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pubmed:affiliation |
Department of Physiology and Biophysics, Boston University School of Medicine, 700 Albany Street, Boston, MA 02118, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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