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Titolo:
Genetic interactions within TFIIIC, the promoter-binding factor of yeast RNA polymerase III
Autore:
Rozenfeld, S; Thuriaux, P;
Indirizzi:
CEA Saclay, Serv Biochim & Genet Mol, F-91191 Gif Sur Yvette, France CEA Saclay Gif Sur Yvette France F-91191 F-91191 Gif Sur Yvette, France
Titolo Testata:
MOLECULAR GENETICS AND GENOMICS
fascicolo: 4, volume: 265, anno: 2001,
pagine: 705 - 710
SICI:
1617-4615(200106)265:4<705:GIWTTP>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSCRIPTION FACTOR-TAU; 2ND LARGEST SUBUNIT; DNA-BINDING; SACCHAROMYCES-CEREVISIAE; TETRATRICOPEPTIDE REPEATS; MUTATION; CLONING; COMPLEX; ACTIVATION; EXPRESSION;
Keywords:
yeast; transfer RNAs; tetratricopeptide; TFIIIB; transcription;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Thuriaux, P CEA Saclay, Serv Biochim & Genet Mol, Bat 142,, F-91191 Gif Sur Yvette, France CEA Saclay Bat 142, Gif Sur Yvette France F-91191 tte, France
Citazione:
S. Rozenfeld e P. Thuriaux, "Genetic interactions within TFIIIC, the promoter-binding factor of yeast RNA polymerase III", MOL GENET G, 265(4), 2001, pp. 705-710

Abstract

TFIIIC is a heteromultimeric protein, made of six distinct subunits in Saccharomyces cerevisiae, that binds to RNA polymerase III promoters and triggers the assembly of the transcription complex. The largest yeast subunit tau138, encoded by TFC3, binds to the B-box promoter element. This binding isdefective in the temperature-sensitive mutant tfc3-G349E; the mutation responsible is located in one of two conserved motifs shared with the B-binding component of human TFIIIC. Rare dominant gain-of-function mutations that restore growth at high temperature were obtained following ultraviolet mutagenesis of tfc3-G349E. All of them resulted from single amino acid substitutions that alter the structure of TFIIIC. Three were due to reversion or intragenic suppression (TFC3-K754E and TFC3-L804H) events. Three were identical isolates of TFC6-E330K, a previously described mutation of the tau91 subunit. The remaining suppressors mapped in TFC4, and resulted in amino acid replacements in the second largest subunit of TFIIIC (tau131). With the exception TFC4-E711K, these affect positions that are invariant between the S.cerevisiae and Homo sapiens proteins, and are localised in conserved tetratricopeptide motifs. These findings demonstrate a close functional interaction between the two largest subunits of TFIIIC and underscore the importance of the tetratricopeptide motif of tau131.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/07/20 alle ore 17:39:03