The nucleolar remodeling complex NoRC mediates heterochromatin formation and silencing of ribosomal gene transcription

2002 ◽  
Vol 32 (3) ◽  
pp. 393-396 ◽  
Author(s):  
Raffaella Santoro ◽  
Junwei Li ◽  
Ingrid Grummt
2005 ◽  
Vol 280 (47) ◽  
pp. 39436-39447 ◽  
Author(s):  
Keiko Shimono ◽  
Yohei Shimono ◽  
Kaoru Shimokata ◽  
Naoki Ishiguro ◽  
Masahide Takahashi

Chromosoma ◽  
1988 ◽  
Vol 96 (6) ◽  
pp. 411-416 ◽  
Author(s):  
Kathleen M. Rose ◽  
Jan Szopa ◽  
Fu-Sheng Han ◽  
Yung-Chi Cheng ◽  
Arndt Richter ◽  
...  

Oncogene ◽  
1999 ◽  
Vol 18 (4) ◽  
pp. 1119-1124 ◽  
Author(s):  
Andreja Budde ◽  
Ingrid Grummt

1994 ◽  
Vol 14 (3) ◽  
pp. 2011-2020
Author(s):  
P Labhart

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.


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