Adrenocorticotropic hormone rgulation of adrenal RNA polymerases. Stimulation of nuclear RNA polymerase III

Biochemistry ◽  
1976 ◽  
Vol 15 (25) ◽  
pp. 5520-5527 ◽  
Author(s):  
Shella A. Fuhrman ◽  
Gordon N. Gill
1987 ◽  
Vol 262 (1) ◽  
pp. 75-81
Author(s):  
R Reddy ◽  
D Henning ◽  
G Das ◽  
M Harless ◽  
D Wright

1996 ◽  
Vol 16 (3) ◽  
pp. 892-898 ◽  
Author(s):  
D J Hockman ◽  
M C Schultz

Casein kinase II (CKII) is a ubiquitous and highly conserved serine/threonine protein kinase found in the nucleus and cytoplasm of most cells. Using a combined biochemical and genetic approach in the yeast Saccharomyces cerevisiae, we assessed the role of CKII in specific transcription by RNA polymerases I, II, and III. CKII is not required for basal transcription by RNA polymerases I and II but is important for polymerase III transcription. Polymerase III transcription is high in extracts with normal CKII activity but low in extracts from a temperature-sensitive mutant that has decreased CKII activity due to a lesion in the enzyme's catalytic alpha' subunit. Polymerase III transcription of 5S rRNA and tRNA templates in the temperature-sensitive extract is rescued by purified, wild-type CKII. An inhibitor of CKII represses polymerase III transcription in wild-type extract, and this repression is partly overcome by supplementing reaction mixtures with active CKII. Finally, we show that polymerase III transcription in vivo is impaired when CKII is inactivated. Our results demonstrate that CKII, an oncogenic protein kinase previously implicated in cell cycle and growth control, is required for high-level transcription by RNA polymerase III.


1992 ◽  
Vol 47 (3-4) ◽  
pp. 320-322 ◽  
Author(s):  
Przemyslaw Szafranski ◽  
W. Jerzy Smagowicz

Abstract Apparent Michaelis constants for nucleotides in transcription of yeast tRN Agene by hom ologous RNA polymerase III with auxiliary protein factors, were found to be remarkably higher in initiation than in elongation of RNA chain. This supports presumptions regarding topological similarities between catalytic centers of bacterial and eukaryotic RNA polymerases.


DNA Repair ◽  
2009 ◽  
Vol 8 (5) ◽  
pp. 620-626 ◽  
Author(s):  
M.C. Díaz de la Loza ◽  
R.E. Wellinger ◽  
A. Aguilera

AGE ◽  
1983 ◽  
Vol 6 (4) ◽  
pp. 106-112 ◽  
Author(s):  
Patricia Fitzpatrick-Dimond ◽  
John A. Todhunter ◽  
Sameeh S. Elridi

2016 ◽  
Author(s):  
Shrivani Sriskanthadevan-Pirahas ◽  
Rujuta Deshpande ◽  
Byoungchun Lee ◽  
Savraj S. Grewal

ABSTRACTThe small G-protein Ras is a conserved regulator of cell and tissue growth. These effects of Ras are mediated largely through activation of a canonical RAF-MEK-ERK kinase cascade. An important challenge is to identify how this Ras/ERK pathway alters cellular metabolism to drive growth. Here we report on stimulation of RNA polymerase III (Pol III)-mediated tRNA synthesis as a growth effector of Ras/ERK signalling in Drosophila. We find that activation of Ras/ERK signalling promotes tRNA synthesis both in vivo and in cultured Drosophila S2 cells. We also show that Pol III function is required for Ras/ERK signalling to drive proliferation in both epithelial and stem cells in Drosophila tissues. We find that the transcription factor Myc is required but not sufficient for Ras-mediated stimulation of tRNA synthesis. Instead we show that the main way that Ras promotes Pol III function and tRNA synthesis is by inhibiting the nuclear localization and function of the Pol III repressor Maf1. We propose that inhibition of Maf1 and stimulation of tRNA synthesis is one way by which Ras signalling enhances protein synthesis to promote cell and tissue growth.


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