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Titolo:
Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new14 kDa Sm D1-like protein
Autore:
Pillai, RS; Will, CL; Luhrmann, R; Schumperli, D; Muller, B;
Indirizzi:
Univ Bern, Inst Cell Biol, CH-3012 Bern, Switzerland Univ Bern Bern Switzerland CH-3012 Cell Biol, CH-3012 Bern, Switzerland Max Planck Inst Biophys Chem, D-37070 Gottingen, Germany Max Planck Inst Biophys Chem Gottingen Germany D-37070 ottingen, Germany Univ Aberdeen, Inst Med Sci, Dept Mol & Cell Biol, Aberdeen AB25 2ZD, Scotland Univ Aberdeen Aberdeen Scotland AB25 2ZD ol, Aberdeen AB25 2ZD, Scotland
Titolo Testata:
EMBO JOURNAL
fascicolo: 19, volume: 20, anno: 2001,
pagine: 5470 - 5479
SICI:
0261-4189(20011001)20:19<5470:PUSLTS>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
PRE-MESSENGER-RNA; SMALL NUCLEAR-RNA; COILED BODIES; U6 SNRNA; RIBONUCLEOPROTEIN-PARTICLES; SPLICEOSOMAL SNRNPS; STRUCTURAL DOMAIN; BINDING-SITE; IN-VITRO; IDENTIFICATION;
Keywords:
Cajal; coiled bodies; histone pre-mRNA 3 ' processing; Sm core structure; Sm-like protein; small nuclear ribonucleoprotein;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Schumperli, D Univ Bern, Inst Cell Biol, Baltzerstr 4, CH-3012 Bern, Switzerland Univ Bern Baltzerstr 4 Bern Switzerland CH-3012 Switzerland
Citazione:
R.S. Pillai et al., "Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new14 kDa Sm D1-like protein", EMBO J, 20(19), 2001, pp. 5470-5479

Abstract

U7 snRNPs; were isolated from HeLa cells by biochemical fractionation, followed by affinity purification with a biotinylated oligonucleotide complementary to U7 snRNA. Purified U7 snRNPs lack the Sm proteins D1 and D2, but contain additional polypeptides of 14, 50 and 70 kDa. Microsequencing identified the 14 kDa polypeptide as a new Sm-like protein related to Sm D1 and D3. Like U7 snRNA, this protein, named Lsm10, is enriched in Cajal bodies ofthe cell nucleus. Its incorporation into U7 snRNPs; is largely dictated bythe special Sm binding site of U7 snRNA. This novel type of Sm complex, composed of both conventional Sm proteins and the Sm-like Lsm10, is most likely to be important for U7 snRNP function and subcellular localization.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 05:27:52