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Titolo:
The crystal structure of nucleoplasmin-core: Implications for histone binding and nucleosome assembly
Autore:
Dutta, S; Akey, IV; Dingwall, C; Hartman, KL; Laue, T; Nolte, RT; Head, JF; Akey, CW;
Indirizzi:
Boston Univ, Sch Med, Dept Physiol & Biophys, Boston, MA 02118 USA Boston Univ Boston MA USA 02118 t Physiol & Biophys, Boston, MA 02118 USA GlaxoSmithKline, Neurobiol, CEDD, Harlow CM19 5AW, Essex, England GlaxoSmithKline Harlow Essex England CM19 5AW ow CM19 5AW, Essex, England Univ New Hampshire, Dept Biochem & Mol Biol, Durham, NH 03824 USA Univ NewHampshire Durham NH USA 03824 m & Mol Biol, Durham, NH 03824 USA GlaxoSmithKline Res & Dev, Dept Struct Chem, Res Triangle Pk, NC 27709 USAGlaxoSmithKline Res & Dev Res Triangle Pk NC USA 27709 e Pk, NC 27709 USA
Titolo Testata:
MOLECULAR CELL
fascicolo: 4, volume: 8, anno: 2001,
pagine: 841 - 853
SICI:
1097-2765(200110)8:4<841:TCSONI>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
XENOPUS-LAEVIS OOCYTES; SPERM DECONDENSATION; CHROMATIN STRUCTURE; ACIDIC PROTEIN; EGG EXTRACTS; INVITRO; NUCLEI; PURIFICATION; COMPLEXES; TRANSCRIPTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Akey, CW Boston Univ, Sch Med, Dept Physiol & Biophys, 700 Albany St, Boston, MA 02118 USA Boston Univ 700 Albany St Boston MA USA 02118 oston, MA 02118 USA
Citazione:
S. Dutta et al., "The crystal structure of nucleoplasmin-core: Implications for histone binding and nucleosome assembly", MOL CELL, 8(4), 2001, pp. 841-853

Abstract

The efficient assembly of histone complexes and nucleosomes requires the participation of molecular chaperones. Currently, there is a paucity of dataon their mechanism of action. We now present the structure of an N-terminal domain of nucleoplasmin (Np-core) at 2.3 Angstrom resolution. The Np-coremonomer 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 histonestorage, sperm chromatin decondensation, and nucleosome assembly.

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Documento generato il 04/04/20 alle ore 02:51:56