scholarly journals Binding of Liganded Vitamin D Receptor to the Vitamin D Receptor Interacting Protein Coactivator Complex Induces Interaction with RNA Polymerase II Holoenzyme

2000 ◽  
Vol 275 (15) ◽  
pp. 10719-10722 ◽  
Author(s):  
Natsuko Chiba ◽  
Zalman Suldan ◽  
Leonard P. Freedman ◽  
Jeffrey D. Parvin
Genetics ◽  
2001 ◽  
Vol 157 (1) ◽  
pp. 17-26 ◽  
Author(s):  
Ya-Wen Chang ◽  
Susie C Howard ◽  
Yelena V Budovskaya ◽  
Jasper Rine ◽  
Paul K Herman

Abstract Saccharomyces cerevisiae cells enter into a distinct resting state, known as stationary phase, in response to specific types of nutrient deprivation. We have identified a collection of mutants that exhibited a defective transcriptional response to nutrient limitation and failed to enter into a normal stationary phase. These rye mutants were isolated on the basis of defects in the regulation of YGP1 expression. In wild-type cells, YGP1 levels increased during the growth arrest caused by nutrient deprivation or inactivation of the Ras signaling pathway. In contrast, the levels of YGP1 and related genes were significantly elevated in the rye mutants during log phase growth. The rye defects were not specific to this YGP1 response as these mutants also exhibited multiple defects in stationary phase properties, including an inability to survive periods of prolonged starvation. These data indicated that the RYE genes might encode important regulators of yeast cell growth. Interestingly, three of the RYE genes encoded the Ssn/Srb proteins, Srb9p, Srb10p, and Srb11p, which are associated with the RNA polymerase II holoenzyme. Thus, the RNA polymerase II holoenzyme may be a target of the signaling pathways responsible for coordinating yeast cell growth with nutrient availability.


Nature ◽  
1996 ◽  
Vol 380 (6569) ◽  
pp. 82-85 ◽  
Author(s):  
David M. Chao ◽  
Ellen L. Gadbois ◽  
Peter J. Murray ◽  
Stephen F. Anderson ◽  
Michelle S. Sonu ◽  
...  

1997 ◽  
Vol 94 (11) ◽  
pp. 5605-5610 ◽  
Author(s):  
R. Scully ◽  
S. F. Anderson ◽  
D. M. Chao ◽  
W. Wei ◽  
L. Ye ◽  
...  

1998 ◽  
Vol 273 (47) ◽  
pp. 30851-30854 ◽  
Author(s):  
Claes M. Gustafsson ◽  
Lawrence C. Myers ◽  
Jenny Beve ◽  
Henrik Spåhr ◽  
Mary Lui ◽  
...  

1977 ◽  
Vol 164 (1) ◽  
pp. 83-89 ◽  
Author(s):  
K W Colston ◽  
I M A Evans ◽  
T C Spelsberg ◽  
I MacIntyre

Many factors influence the production of 1,25(OH)2D3 (1,25-dihydroxycholecalciferol) by the kidney. One important factor seems to be feedback regulation by 1,25(OH)2D3 itself. Administration of 1,25(OH)2D3 to vitamin D-deficient chicks abolishes renal 25(OH)D3(25-hydroxycholecalciferol)1-hydroxylase activity and induces the appearance of 25(OH)D3 24-hydroxylase activity. It is likely that these effects are mediated via a nuclear effect, as they are prevented by pretreatment with actinomycin D and alpha-amanitin. Further, 1,25(OH)2D3 has a marked effect on gene transcription in the kidney cell, as assessed by measurement of RNA polymerase activities. RNA polymerase I and II activities are 80-90% inhibited by 12.5nmol of 1,25(OH)2D3 within 30min of subcutaneous administration, indicating an immediate and massive decrease in total gene transcription. By 4h RNA polymerase II activity has returned to control values, but RNA polymerase I activity is markedly enhanced. These results are consistent with the view that regulation of cholecalciferol metabolism in the kidney is associated with an effect of the active metabolite on the kidney nucleus.


1995 ◽  
Vol 9 (8) ◽  
pp. 897-910 ◽  
Author(s):  
C J Hengartner ◽  
C M Thompson ◽  
J Zhang ◽  
D M Chao ◽  
S M Liao ◽  
...  

1998 ◽  
Vol 18 (5) ◽  
pp. 2876-2883 ◽  
Author(s):  
Song He ◽  
Steven Jay Weintraub

ABSTRACT Recently, it was found that if either the TATA binding protein or RNA polymerase II holoenzyme is artificially tethered to a promoter, transcription is activated. This finding provided presumptive evidence that upstream activating proteins function by recruiting components of the preinitiation complex (PIC) to the promoter. To date, however, there have been no studies demonstrating that upstream factors actually recruit components of the PIC to the promoter in vivo. Therefore, we have studied the mechanism of action of two disparate transactivating domains. We present a series of in vivo functional assays that demonstrate that each of these proteins targets different components of the PIC for recruitment. We show that, by targeting different components of the PIC for recruitment, these activating domains can cooperate with each other to activate transcription synergistically and that, even within one protein, two different activating subdomains can activate transcription synergistically by cooperating to recruit different components of the PIC. Finally, considering our work together with previous studies, we propose that certain transcription factors both recruit components of the PIC and facilitate steps in transcriptional activation that occur subsequent to recruitment.


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