scholarly journals DNA-dependent protein kinase specifically represses promoter-directed transcription initiation by RNA polymerase I.

1995 ◽  
Vol 92 (7) ◽  
pp. 2934-2938 ◽  
Author(s):  
P. Labhart
Keyword(s):  
Protein Kinase ◽  
Rna Polymerase ◽  
Transcription Initiation ◽  
Rna Polymerase I ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Polymerase I

scholarly journals DNA-dependent protein kinase: a potent inhibitor of transcription by RNA polymerase I.

1995 ◽  
Vol 9 (2) ◽  
pp. 193-203 ◽  
Author(s):  
A Kuhn ◽  
T M Gottlieb ◽  
S P Jackson ◽  
I Grummt
Keyword(s):  
Protein Kinase ◽  
Rna Polymerase ◽  
Protein Kinase A ◽  
Potent Inhibitor ◽  
Rna Polymerase I ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Polymerase I ◽  
Kinase A

Identification of two steps during Xenopus ribosomal gene transcription that are sensitive to protein phosphorylation

1994 ◽  
Vol 14 (3) ◽  
pp. 2011-2020
Author(s):  
P Labhart
Keyword(s):  
Protein Kinase ◽  
Rna Polymerase ◽  
Protein Phosphorylation ◽  
Gene Transcription ◽  
Okadaic Acid ◽  
Protein Phosphatase ◽  
Transcription Initiation ◽  
Ribosomal Gene ◽  
Rna Polymerase I ◽  
Polymerase I

Protein kinase(s) and protein phosphatase(s) present in a Xenopus S-100 transcription extract strongly influence promoter-dependent transcription by RNA polymerase I. The protein kinase inhibitor 6-dimethyl-aminopurine causes transcription to increase, while the protein phosphatase inhibitor okadaic acid causes transcription to decrease. Repression is also observed with inhibitor 2, and the addition of extra protein phosphatase 1 stimulates transcription, indicating that the endogenous phosphatase is a type 1 enzyme. Partial fractionation of the system, single-round transcription reactions, and kinetic experiments show that two different steps during ribosomal gene transcription are sensitive to protein phosphorylation: okadaic acid affects a step before or during transcription initiation, while 6-dimethylaminopurine stimulates a process "late" in the reaction, possibly reinitiation. The present results are a clear demonstration that transcription by RNA polymerase I can be regulated by protein phosphorylation.

scholarly journals Identification of two steps during Xenopus ribosomal gene transcription that are sensitive to protein phosphorylation.

1994 ◽  
Vol 14 (3) ◽  
pp. 2011-2020 ◽  
Author(s):  
P Labhart
Keyword(s):  
Protein Kinase ◽  
Rna Polymerase ◽  
Protein Phosphorylation ◽  
Gene Transcription ◽  
Okadaic Acid ◽  
Protein Phosphatase ◽  
Transcription Initiation ◽  
Ribosomal Gene ◽  
Rna Polymerase I ◽  
Polymerase I

Protein kinase(s) and protein phosphatase(s) present in a Xenopus S-100 transcription extract strongly influence promoter-dependent transcription by RNA polymerase I. The protein kinase inhibitor 6-dimethyl-aminopurine causes transcription to increase, while the protein phosphatase inhibitor okadaic acid causes transcription to decrease. Repression is also observed with inhibitor 2, and the addition of extra protein phosphatase 1 stimulates transcription, indicating that the endogenous phosphatase is a type 1 enzyme. Partial fractionation of the system, single-round transcription reactions, and kinetic experiments show that two different steps during ribosomal gene transcription are sensitive to protein phosphorylation: okadaic acid affects a step before or during transcription initiation, while 6-dimethylaminopurine stimulates a process "late" in the reaction, possibly reinitiation. The present results are a clear demonstration that transcription by RNA polymerase I can be regulated by protein phosphorylation.

Events during eucaryotic rRNA transcription initiation and elongation: conversion from the closed to the open promoter complex requires nucleotide substrates

1988 ◽  
Vol 8 (5) ◽  
pp. 1940-1946
Author(s):  
E Bateman ◽  
M R Paule
Keyword(s):  
Rna Polymerase ◽  
Transcription Initiation ◽  
Topological Analysis ◽  
Acanthamoeba Castellanii ◽  
Rna Polymerase I ◽  
Initiation Factor ◽  
Rrna Transcription ◽  
Promoter Complex ◽  
Polymerase I

Chemical footprinting and topological analysis were carried out on the Acanthamoeba castellanii rRNA transcription initiation factor (TIF) and RNA polymerase I complexes with DNA during transcription initiation and elongation. The results show that the binding of TIF and polymerase to the promoter does not alter the supercoiling of the DNA template and the template does not become sensitive to modification by diethylpyrocarbonate, which can identify melted DNA regions. Thus, in contrast to bacterial RNA polymerase, the eucaryotic RNA polymerase I-promoter complex is in a closed configuration preceding addition of nucleotides in vitro. Initiation and 3'-O-methyl CTP-limited translocation by RNA polymerase I results in separation of the polymerase-TIF footprints, leaving the TIF footprint unaltered. In contrast, initiation and translocation result in a significant change in the conformation of the polymerase-DNA complex, culminating in an unwound DNA region of at least 10 base pairs.

scholarly journals Promoter opening (melting) and transcription initiation by RNA polymerase I requires neither nucleotideβ,γhydrolysis norprotein phosphorylation

1993 ◽  
Vol 21 (14) ◽  
pp. 3233-3238 ◽  
Author(s):  
Alan K. Logquist ◽  
Han Li ◽  
Martin lmboden ◽  
Marvin R. Paule
Keyword(s):  
Rna Polymerase ◽  
Transcription Initiation ◽  
Rna Polymerase I ◽  
Polymerase I
Sign in / Sign up

Export Citation Format

Share Document