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Titolo:
THE SPECIES-SPECIFIC RNA-POLYMERASE-I TRANSCRIPTION FACTOR SL-1 BINDSTO UPSTREAM BINDING-FACTOR
Autore:
HEMPEL WM; CAVANAUGH AH; HANNAN RD; TAYLOR L; ROTHBLUM LI;
Indirizzi:
WEIS CTR RES,GEISINGER CLIN DANVILLE PA 17822 WEIS CTR RES,GEISINGER CLIN DANVILLE PA 17822
Titolo Testata:
Molecular and cellular biology
fascicolo: 2, volume: 16, anno: 1996,
pagine: 557 - 563
SICI:
0270-7306(1996)16:2<557:TSRTFS>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
RAT RIBOSOMAL DNA; FACTOR UBF; ACTIVATION DOMAIN; RDNA PROMOTER; FACTOR XUBF; FACTOR HUBF; GENE; INITIATION; PHOSPHORYLATION; TRANSACTIVATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
47
Recensione:
Indirizzi per estratti:
Citazione:
W.M. Hempel et al., "THE SPECIES-SPECIFIC RNA-POLYMERASE-I TRANSCRIPTION FACTOR SL-1 BINDSTO UPSTREAM BINDING-FACTOR", Molecular and cellular biology, 16(2), 1996, pp. 557-563

Abstract

Transcription of the 45S rRNA genes is carried out by RNA polymerase I and at least two trans-acting factors, upstream binding factor (UBF)and SL-1. We have examined the hypothesis that SL-I and UBF interact. Coimmunoprecipitation studies using an antibody to UBF demonstrated that TATA-binding protein, a subunit of SL-1, associates with UBF in the absence of DNA. Inclusion of the detergents sodium dodecyl sulfate and deoxycholate disrupted this interaction. In addition, partially purified UBF from rat cell nuclear extracts and partially purified SL-1 from human cells coimmunoprecipitated with the anti-UBF antibody after mixing, indicating that the UBF-SL-1 complex can re-form. Treatment ofUBF-depleted extracts with the anti-UBF antibody depleted the extracts of SL-1 activity only if UBF was added to the extract prior to the immunodepletion reaction. Furthermore, SL-1 activity could be recoveredin the immunoprecipitate. Interestingly, these immunoprecipitates didnot contain RNA polymerase I, as a monospecific antibody to the 194-kDa subunit of RNA polymerase I failed to detect that subunit in the immunoprecipitates. Treatment of N1S1 cell extracts with the anti-UBF antibody depleted the extracts of SL-1 activity but not TFIIIB activity,suggesting that the binding of UBF to SL-1 is specific and not solelymediated by an interaction between UBF and TATA-binding protein, which is also a component of TFIIIB. These data provide evidence that UBF and SL-1 interact.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/09/20 alle ore 16:56:25