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Titolo:
CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression
Autore:
Stauffer, DR; Howard, TL; Nyun, T; Hollenberg, SM;
Indirizzi:
Oregon Hlth Sci Univ, Vollum Inst, Portland, OR 97201 USA Oregon Hlth Sci Univ Portland OR USA 97201 m Inst, Portland, OR 97201 USA
Titolo Testata:
JOURNAL OF CELL SCIENCE
fascicolo: 13, volume: 114, anno: 2001,
pagine: 2383 - 2393
SICI:
0021-9533(200107)114:13<2383:CIANNM>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
POLYCOMB-GROUP PROTEINS; MITOTIC CHROMOSOME CONDENSATION; HISTONE H3 PHOSPHORYLATION; CAENORHABDITIS-ELEGANS; DROSOPHILA-MELANOGASTER; BITHORAX COMPLEX; GENE-EXPRESSION; B-DNA; REPRESSION; DOMAIN;
Keywords:
MeSH; gene silencing; nuclear matrix; chromatin; histories; DNA replication; S phase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
65
Recensione:
Indirizzi per estratti:
Indirizzo: Stauffer, DR Oregon Hlth Sci Univ, Vollum Inst, L474,3181 SW Sam Jackson Pk Rd, Portland, OR 97201 USA Oregon Hlth Sci Univ L474,3181 SW Sam Jackson Pk Rd Portland OR USA 97201
Citazione:
D.R. Stauffer et al., "CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression", J CELL SCI, 114(13), 2001, pp. 2383-2393

Abstract

The Polycomb-group (PcG) is a diverse set of proteins required for maintenance of gene silencing during development. In a screen for conserved partners of the PcG protein Polycomblike (Pcl), we have identified a new protein,human CHMP1 (CHromatin Modifying Protein; CHarged Multivesicular body Protein), which is encoded by an alternative open reading frame in the PRSM1 gene and is conserved in both complex and simple eukaryotes. CHMP1 contains apredicted bipartite nuclear localization signal and distributes as distinct forms to the cytoplasm and the nuclear matrix in all cell lines tested. We have constructed a stable HEK293 cell line that inducibly overexpresses CHMP1 under ecdysone control. Overexpressed CHMP1 localizes to a punctate subnuclear pattern, encapsulating regions of nuclease-resistant, condensed chromatin. These novel structures are also frequently surrounded by increasedhistone H3 phosphorylation and acetylation. CHMP1 can recruit a PcG protein, BMI1, to these regions of condensed chromatin and can cooperate with co-expressed vertebrate Pcl in a Xenopus embryo PcG assay; this is consistent with a role in PcG function. In combination, these observations suggest that CHMP1 plays a role in stable gene silencing within the nucleus.

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Documento generato il 04/12/20 alle ore 13:19:30