Stimulation of guanylate cyclase and RNA polymerase II activities in HeLa cells and fibroblasts by biotin

1988 ◽  
Vol 79 (1) ◽  
pp. 47-55 ◽  
Author(s):  
Indrapal N. Singh ◽  
Kirshnamurti Dakshinamurti
Science ◽  
1994 ◽  
Vol 265 (5173) ◽  
pp. 796-799 ◽  
Author(s):  
H. Ding ◽  
S Rimsky ◽  
S. Batson ◽  
M Bustin ◽  
U Hansen

Biochemistry ◽  
1991 ◽  
Vol 30 (31) ◽  
pp. 7842-7851 ◽  
Author(s):  
Kan Agarwal ◽  
KwangHee Baek ◽  
ChoonJu Jeon ◽  
Kenichi Miyamoto ◽  
Akemichi Ueno ◽  
...  

2003 ◽  
Vol 23 (17) ◽  
pp. 6229-6242 ◽  
Author(s):  
Shwu-Yuan Wu ◽  
Tianyuan Zhou ◽  
Cheng-Ming Chiang

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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