Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
AFFINITY PURIFICATION OF MAMMALIAN RNA-POLYMERASE-I - IDENTIFICATION OF AN ASSOCIATED KINASE
Autore:
HANNAN RD; HEMPEL WM; CAVANAUGH A; ARINO T; DIMITROV SI; MOSS T; ROTHBLUM L;
Indirizzi:
WEIS CTR RES,GEISINGER CLIN,HENRY HOOD RES PROGRAM DANVILLE PA 17822 WEIS CTR RES,GEISINGER CLIN,HENRY HOOD RES PROGRAM DANVILLE PA 17822 UNIV LAVAL,HOTEL DIEU,CANC RES CTR QUEBEC CITY PQ G1R 2J6 CANADA
Titolo Testata:
The Journal of biological chemistry
fascicolo: 2, volume: 273, anno: 1998,
pagine: 1257 - 1267
SICI:
0021-9258(1998)273:2<1257:APOMR->2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSCRIPTION FACTOR UBF; RAT RIBOSOMAL DNA; FACTOR-TIF-IA; CASEIN KINASE; LARGEST SUBUNIT; LYMPHOSARCOMA-P1798 CELLS; SACCHAROMYCES-CEREVISIAE; 2ND-LARGEST SUBUNIT; HORMONAL-REGULATION; RDNA TRANSCRIPTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
82
Recensione:
Indirizzi per estratti:
Citazione:
R.D. Hannan et al., "AFFINITY PURIFICATION OF MAMMALIAN RNA-POLYMERASE-I - IDENTIFICATION OF AN ASSOCIATED KINASE", The Journal of biological chemistry, 273(2), 1998, pp. 1257-1267

Abstract

Overlapping cDNA clones encoding the two largest subunits of rat RNA polymerase I, designated A194 and A127, were isolated from a Reuber hepatoma cDNA library. Analyses of the deduced amino acid Sequences revealed that A194 and A127 are the homologues of yeast A190 and A135 and have homology to the beta' and beta subunits of Escherichia coli RNA polymerase I. Antibodies raised against the recombinant A194 and A127 proteins recognized single proteins of approximately 190 and 120 kDa onWestern blots of total cellular proteins of mammalian origin. N1S1 cell lines expressing recombinant His tagged A194 and FLAG-tagged A127 proteins were isolated, These proteins were incorporated into functional RNA polymerase I complexes, and active enzyme, containing FLAG-tagged A127, could be immunopurified to approximately 80% homogeneity in a single chromatographic step over an anti-FLAG affinity column, Immunoprecipitation of A194 from P-32 metabolically labeled cells with anti-A194 antiserum demonstrated that this subunit is a phosphoprotein. Incubation of the FLAG affinity-purified RNA polymerase I complex with [gamma-P-32]ATP resulted in autophosphorylation of the A194 subunit of RPI, indicating the presence of associated kinase(s). One of these kinases was demonstrated to be CK2, a serine/threonine protein kinase implicated in the regulation of cell growth and proliferation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/09/20 alle ore 16:50:51