BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A

10.1038/930 ◽  
1998 ◽  
Vol 19 (3) ◽  
pp. 254-256 ◽  
Author(s):  
Stephen F. Anderson ◽  
Brian P. Schlegel ◽  
Toshihiro Nakajima ◽  
Eric S. Wolpin ◽  
Jeffrey D. Parvin
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Rna Helicase ◽  
Rna Helicase A ◽  
Brca1 Protein ◽  
Rna Polymerase Ii Holoenzyme

RNA helicase A acts as a bridging factor linking nuclear β-actin with RNA polymerase II

2009 ◽  
Vol 420 (3) ◽  
pp. 421-428 ◽  
Author(s):  
Wen Tang ◽  
Wanhui You ◽  
Feng Shi ◽  
Tianyang Qi ◽  
Ling Wang ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Transcription Initiation ◽  
Glutathione Transferase ◽  
Rna Helicase ◽  
Dominant Negative ◽  
Dominant Negative Mutant ◽  
Rna Helicase A ◽  
Interacting Protein ◽  
Pol Ii

Actin, the major component of the cytoplasmic skeleton, has been shown to exist in the nucleus. Nuclear actin functions in several steps of the transcription process, including chromatin remodelling and transcription initiation and elongation. However, as a part of PICs (pre-initiation complexes), the role of actin remains to be elucidated. In the present study, we identified RHA (RNA helicase A) as an actin-interacting protein in PICs. Using immunoprecipitation and immunofluorescence techniques, we have shown that RHA associates with β-actin in the nucleus. A GST (glutathione transferase) pulldown assay using different deletion mutants revealed that the RGG (Arg-Gly-Gly) region of RHA was responsible for the interaction with β-actin, and this dominant-negative mutant reduced the recruitment of Pol II (RNA polymerase II) into PICs. Moreover, overexpression or depletion of RHA could influence the interaction of Pol II with β-actin and β-actin-involved gene transcription regulation. These results suggest that RHA acts as a bridging factor linking nuclear β-actin with Pol II.

scholarly journals RNA Helicase A Mediates Association of CBP with RNA Polymerase II

Cell ◽  
1997 ◽  
Vol 90 (6) ◽  
pp. 1107-1112 ◽  
Author(s):  
Toshihiro Nakajima ◽  
Chiharu Uchida ◽  
Stephen F. Anderson ◽  
Chee-Gun Lee ◽  
Jerard Hurwitz ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Rna Helicase ◽  
Rna Helicase A

scholarly journals The rye Mutants Identify a Role for Ssn/Srb Proteins of the RNA Polymerase II Holoenzyme During Stationary Phase Entry in Saccharomyces cerevisiae

Genetics ◽  
2001 ◽  
Vol 157 (1) ◽  
pp. 17-26 ◽  
Author(s):  
Ya-Wen Chang ◽  
Susie C Howard ◽  
Yelena V Budovskaya ◽  
Jasper Rine ◽  
Paul K Herman
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Growth ◽  
Rna Polymerase ◽  
Stationary Phase ◽  
Yeast Cell ◽  
Rna Polymerase Ii ◽  
Transcriptional Response ◽  
Nutrient Deprivation ◽  
Ras Signaling ◽  
Rna Polymerase Ii Holoenzyme

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.

A mammalian SRB protein associated with an RNA polymerase II holoenzyme

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 ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Rna Polymerase Ii Holoenzyme

scholarly journals BRCA1 is a component of the RNA polymerase II holoenzyme

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

scholarly journals Identification of New Mediator Subunits in the RNA Polymerase II Holoenzyme fromSaccharomyces cerevisiae

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

scholarly journals Association of an activator with an RNA polymerase II holoenzyme.

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

scholarly journals Stepwise Recruitment of Components of the Preinitiation Complex by Upstream Activators In Vivo

1998 ◽  
Vol 18 (5) ◽  
pp. 2876-2883 ◽  
Author(s):  
Song He ◽  
Steven Jay Weintraub
Keyword(s):  
Transcription Factors ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Mechanism Of Action ◽  
Transcriptional Activation ◽  
Tata Binding Protein ◽  
Preinitiation Complex ◽  
Functional Assays ◽  
Rna Polymerase Ii Holoenzyme

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.

Sign in / Sign up

Export Citation Format

Share Document