Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
A review of progress towards elucidating the role of protein kinase CK2 inpolymerase III transcription: Regulation of the TATA binding protein
Autore:
Ghavidel, A; Hockman, DJ; Schultz, MC;
Indirizzi:
Univ Alberta, Dept Biochem, Edmonton, AB T6G 2H7, Canada Univ Alberta Edmonton AB Canada T6G 2H7 hem, Edmonton, AB T6G 2H7, Canada
Titolo Testata:
MOLECULAR AND CELLULAR BIOCHEMISTRY
fascicolo: 1-2, volume: 191, anno: 1999,
pagine: 143 - 148
SICI:
0300-8177(199901)191:1-2<143:AROPTE>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
SACCHAROMYCES-CEREVISIAE; CELL-CYCLE; MITOTIC REPRESSION; GENE-TRANSCRIPTION; YEAST; PHOSPHORYLATION; TFIIIB; DISRUPTION; COMPLEXES; SUBUNIT;
Keywords:
transcription; RNA polymerase III; casein kinase II; CK2; TATA binding protein; TFIIIB;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Schultz, MC Univ Alberta, Dept Biochem, Edmonton, AB T6G 2H7, Canada Univ Alberta Edmonton AB Canada T6G 2H7 n, AB T6G 2H7, Canada
Citazione:
A. Ghavidel et al., "A review of progress towards elucidating the role of protein kinase CK2 inpolymerase III transcription: Regulation of the TATA binding protein", MOL C BIOCH, 191(1-2), 1999, pp. 143-148

Abstract

We have investigated the molecular basis of the requirement for protein kinase CK2 in nuclear transcription in Saccharomyces cerevisiae. In vivo and in vitro analysis has demonstrated that CK2 is required for efficient transcription of the tRNA and 55 rRNA genes by RNA polymerase III. This suggeststhat a component of the pol III transcription machinery is regulated by CK2. We tested this possibility by a biochemical complementation approach in which components of the pol III transcription machinery from wild type cells were tested for their ability to rescue transcription in extract from a conditionally CK2-deficient mutant. We found that pol III transcription initiation factor IIIB (TFIIIB) fully restores transcription in CK2-deficient extract. Further in vitro studies revealed that TFIIIB must be phosphorylated to be active, that a single subunit of wild type TFIIIB, the TATA bindingprotein (TBP), is efficiently phosphorylated by CK2, and that recombinant TBP and a limiting amount of CK2 rescues transcription in CK2-deficient extract. We conclude that TBP is the physiological target of CK2 among the components of the pol III transcription machinery. The implications of this result are discussed in the context of previous data concerning the regulation of TFIIIB.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 06:13:07