scholarly journals Isolation and Characterization ofTAF25, an Essential Yeast Gene That Encodes an RNA Polymerase II-specific TATA-binding Protein-associated Factor

1996 ◽  
Vol 271 (23) ◽  
pp. 13706-13715 ◽  
Author(s):  
Edward R. Klebanow ◽  
David Poon ◽  
Sharleen Zhou ◽  
P. Anthony Weil
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Binding Protein ◽  
Tata Binding Protein ◽  
Yeast Gene ◽  
Associated Factor ◽  
Isolation And Characterization

scholarly journals Regulation of rRNA Synthesis by TATA-Binding Protein-Associated Factor Mot1

2007 ◽  
Vol 27 (8) ◽  
pp. 2886-2896 ◽  
Author(s):  
Arindam Dasgupta ◽  
Rebekka O. Sprouse ◽  
Sarah French ◽  
Pavel Aprikian ◽  
Robert Hontz ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Binding Protein ◽  
Tata Binding Protein ◽  
Rrna Synthesis ◽  
Direct Role ◽  
Pol Ii ◽  
Associated Factor ◽  
Pol I

ABSTRACT Mot1 is an essential, conserved, TATA-binding protein (TBP)-associated factor in Saccharomyces cerevisiae with well-established roles in the global control of RNA polymerase II (Pol II) transcription. Previous results have suggested that Mot1 functions exclusively in Pol II transcription, but here we report a novel role for Mot1 in regulating transcription by RNA polymerase I (Pol I). In vivo, Mot1 is associated with the ribosomal DNA, and loss of Mot1 results in decreased rRNA synthesis. Consistent with a direct role for Mot1 in Pol I transcription, Mot1 also associates with the Pol I promoter in vitro in a reaction that depends on components of the Pol I general transcription machinery. Remarkably, in addition to Mot1's role in initiation, rRNA processing is delayed in mot1 cells. Taken together, these results support a model in which Mot1 affects the rate and efficiency of rRNA synthesis by both direct and indirect mechanisms, with resulting effects on transcription activation and the coupling of rRNA synthesis to processing.

scholarly journals Mediator, TATA-binding Protein, and RNA Polymerase II Contribute to Low Histone Occupancy at Active Gene Promoters in Yeast

2014 ◽  
Vol 289 (21) ◽  
pp. 14981-14995 ◽  
Author(s):  
Suraiya A. Ansari ◽  
Emily Paul ◽  
Sebastian Sommer ◽  
Corinna Lieleg ◽  
Qiye He ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Binding Protein ◽  
Tata Binding Protein ◽  
Gene Promoters ◽  
Active Gene

A multisubunit complex associated with the RNA polymerase II CTD and TATA-binding protein in yeast

Cell ◽  
1993 ◽  
Vol 73 (7) ◽  
pp. 1361-1375 ◽  
Author(s):  
Craig M. Thompson ◽  
Anthony J. Koleske ◽  
David M. Chao ◽  
Richard A. Young
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Binding Protein ◽  
Tata Binding Protein ◽  
Rna Polymerase Ii Ctd

scholarly journals Human Mediator Enhances Activator-Facilitated Recruitment of RNA Polymerase II and Promoter Recognition by TATA-Binding Protein (TBP) Independently of TBP-Associated Factors

2003 ◽  
Vol 23 (17) ◽  
pp. 6229-6242 ◽  
Author(s):  
Shwu-Yuan Wu ◽  
Tianyuan Zhou ◽  
Cheng-Ming Chiang
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Associated Factors ◽  
Binding Protein ◽  
Tata Binding Protein ◽  
Dependent Manner ◽  
Basal Transcription ◽  
Pol Ii ◽  
Promoter Recognition ◽  
Stimulation Of

ABSTRACT Mediator is a general cofactor implicated in the functions of many transcriptional activators. Although Mediator with different protein compositions has been isolated, it remains unclear how Mediator facilitates activator-dependent transcription, independent of its general stimulation of basal transcription. To define the mechanisms of Mediator function, we isolated two forms of human Mediator complexes (Mediator-P.5 and Mediator-P.85) and demonstrated that Mediator-P.5 clearly functions by enhancing activator-mediated recruitment of RNA polymerase II (pol II), whereas Mediator-P.85 works mainly by stimulating overall basal transcription. The coactivator function of Mediator-P.5 was not impaired when TATA-binding protein (TBP) was used in place of TFIID, but it was abolished when another general cofactor, PC4, was omitted from the reaction or when Mediator-P.5 was added after pol II entry into the preinitiation complex. Moreover, Mediator- P.5 is able to enhance TBP binding to the TATA box in an activator-dependent manner. Our data provides biochemical evidence that Mediator functions by facilitating activator-mediated recruitment of pol II and also promoter recognition by TBP, both of which can occur in the absence of TBP-associated factors in TFIID.

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