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Titolo:
MOLECULAR CHARACTERIZATION OF A NOVEL, WIDESPREAD NUCLEAR-PROTEIN THAT COLOCALIZES WITH SPLICEOSOME COMPONENTS
Autore:
SCHMIDTZACHMANN MS; KNECHT S; KRAMER A;
Indirizzi:
GERMAN CANC RES CTR,DIV CELL BIOL D-69120 HEIDELBERG GERMANY UNIV GENEVA,DEPT BIOL CELLULAIRE CH-1211 GENEVA 4 SWITZERLAND
Titolo Testata:
Molecular biology of the cell
fascicolo: 1, volume: 9, anno: 1998,
pagine: 143 - 160
SICI:
1059-1524(1998)9:1<143:MCOANW>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
PRE-MESSENGER-RNA; AMINO-ACID-SEQUENCE; SPLICING FACTOR; XENOPUS-LAEVIS; MONOCLONAL-ANTIBODIES; DESMOSOMAL PLAQUE; NUCLEOLAR PROTEIN; BINDING PROTEINS; CULTURED-CELLS; COILED BODIES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
82
Recensione:
Indirizzi per estratti:
Citazione:
M.S. Schmidtzachmann et al., "MOLECULAR CHARACTERIZATION OF A NOVEL, WIDESPREAD NUCLEAR-PROTEIN THAT COLOCALIZES WITH SPLICEOSOME COMPONENTS", Molecular biology of the cell, 9(1), 1998, pp. 143-160

Abstract

We report the identification and molecular characterization of a novel type of constitutive nuclear protein that is present in diverse vertebrate species, from Xenopus laevis to human. The cDNA-deduced amino acid sequence of the Xenopus protein defines a polypeptide of a calculated mass of 146.2 kDa and a isoelectric point of 6.8, with a conspicuous domain enriched in the dipeptide TP (threonine-proline) near its amino terminus. Immunolocalization studies in cultured cells and tissuessections of different origin revealed an exclusive nuclear localization of the protein. The protein is diffusely distributed in the nucleoplasm but concentrated in nuclear speckles, which represent a subnuclear compartment enriched in small nuclear ribonucleoprotein particles and other splicing factors, as confirmed by colocalization with certain splicing factors and Sm proteins. During mitosis, when transcription and splicing are downregulated, the protein is released from the nuclear speckles and transiently dispersed throughout the cytoplasm. Biochemical experiments have shown that the protein is recovered in a similarto 12S complex, and gel filtration studies confirm that the protein is part of a large particle. Immunoprecipitation and Western blot analysis of chromatographic fractions enriched in human U2 small nuclear ribonucleoprotein particles of distinct sizes (12S, 15S, and 17S), reflecting their variable association with splicing factors SF3a and SF3b, strongly suggests that the 146-kDa protein reported here is a constituent of the SF3b complex.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 13:23:07