Testing the Steric Exclusion Model for Hexameric Helicases:  Substrate Features That Alter RNA−DNA Unwinding by the Transcription Termination Factor Rho†

Biochemistry ◽  
2006 ◽  
Vol 45 (18) ◽  
pp. 5885-5895 ◽  
Author(s):  
Céline Walmacq ◽  
A. Rachid Rahmouni ◽  
Marc Boudvillain
Keyword(s):  
Transcription Termination ◽  
Dna Unwinding ◽  
Termination Factor ◽  
Steric Exclusion ◽  
Transcription Termination Factor ◽  
Hexameric Helicases

Bacteriophage T4 Alc protein: A transcription termination factor sensing local modification of DNA

Cell ◽  
1993 ◽  
Vol 75 (1) ◽  
pp. 147-154 ◽  
Author(s):  
Mikhail Kashlev ◽  
Evgeny Nudler ◽  
Alex Goldfarb ◽  
Terry White ◽  
Elizabeth Kutter
Keyword(s):  
Transcription Termination ◽  
Bacteriophage T4 ◽  
Protein A ◽  
Termination Factor ◽  
Transcription Termination Factor ◽  
Local Modification

The mitotically phosphorylated form of the transcription termination factor TTF-1 is associated with the repressed rDNA transcription machinery

1999 ◽  
Vol 112 (19) ◽  
pp. 3259-3268 ◽  
Author(s):  
V. Sirri ◽  
P. Roussel ◽  
D. Hernandez-Verdun
Keyword(s):  
Transcription Termination ◽  
Nucleolar Organizer ◽  
Ribosomal Gene ◽  
Nucleolar Organizer Regions ◽  
Rdna Transcription ◽  
Mitotic Chromosomes ◽  
Termination Factor ◽  
Transcription Machinery ◽  
Phosphorylated Form ◽  
Transcription Termination Factor

The transcription termination factor TTF-1 exerts two functions in ribosomal gene (rDNA) transcription: facilitating initiation and mediating termination of transcription. Using HeLa cells, we show that TTF-1 protein is colocalized with the active transcription machinery in the nucleolus and also with the inactive machinery present in certain mitotic nucleolar organizer regions (NORs) when rDNA transcription is repressed. We also show that TTF-1 is specifically phosphorylated during mitosis in a manner dependent on the cdc2-cyclin B kinase pathway and on an okadaic acid-sensitive phosphatase. Interestingly, the mitotically phosphorylated form of TTF-1 appearing at the G(2)/M transition phase was more easily solubilized than was the interphase form. This indicates that the chromatin-binding affinity of TTF-1 appears to be different in mitotic chromosomes compared to the interphase nucleolus. Correlated with this, the other DNA-binding factor, UBF, which interferes with chromatin conformation in the rDNA promoter, was more strongly bound to rDNA during mitosis than at interphase. The reorganization of the mitotic rDNA promoter might be induced by phosphorylation of certain components of the rDNA transcription machinery and participate in silencing of rDNA during mitosis.

scholarly journals The Structural Basis for Terminator Recognition by the Rho Transcription Termination Factor

1999 ◽  
Vol 3 (4) ◽  
pp. 487-493 ◽  
Author(s):  
Cynthia E. Bogden ◽  
Deborah Fass ◽  
Nick Bergman ◽  
Matthew D. Nichols ◽  
James M. Berger
Keyword(s):  
Transcription Termination ◽  
Structural Basis ◽  
Termination Factor ◽  
Transcription Termination Factor
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