scholarly journals Structural mimicry in transcription regulation of human RNA polymerase II by the DNA helicase RECQL5

2013 ◽  
Vol 20 (7) ◽  
pp. 892-899 ◽  
Author(s):  
Susanne A Kassube ◽  
Martin Jinek ◽  
Jie Fang ◽  
Susan Tsutakawa ◽  
Eva Nogales
2005 ◽  
Vol 13 (1) ◽  
pp. 44-48 ◽  
Author(s):  
Hubert Kettenberger ◽  
Alexander Eisenführ ◽  
Florian Brueckner ◽  
Mirko Theis ◽  
Michael Famulok ◽  
...  

2013 ◽  
Vol 9 (1) ◽  
pp. 638 ◽  
Author(s):  
Astrid Eijkelenboom ◽  
Michal Mokry ◽  
Elzo de Wit ◽  
Lydia M Smits ◽  
Paulien E Polderman ◽  
...  

2002 ◽  
Vol 158 (3) ◽  
pp. 463-473 ◽  
Author(s):  
Beata Fuchsová ◽  
Petr Novák ◽  
Jarmila Kafková ◽  
Pavel Hozák

It is known that nuclear DNA helicase II (NDH II) links CREB-binding protein directly to RNA polymerase II holoenzyme, and that this interaction is essential for gene activation by CREB. Here, we report for the first time that some NDH II/RNA helicase A is a component of promyelocytic leukemia nuclear bodies (PML NBs). An autoimmune serum specific for PML NBs was identified and used in immunoprecipitation experiments. NDH II was present in the immunoprecipitates as shown by mass spectrometry and by immunoblotting. Immunofluorescence and ultrastructural studies showed that NDH II colocalizes with a small subset of PML NBs in control cells, however, colocalizes with practically all bodies in interferon-α–stimulated cells. After interferon stimulation, more PML NBs were found to contain newly synthesized RNA, as indicated by bromouridine incorporation. PML NBs also contain RNA polymerase II. The association of NDH II with PML NBs was transcriptionally dependent, and NDH II was present in all bodies with nascent RNA. Blocking of mRNA synthesis caused NDH II relocalization from nucleoplasm to nucleoli. Based on the data, we suggest that NDH II recruitment to PML NBs is connected with transcriptional regulation of interferon-α–inducible genes attached to PML NBs.


2012 ◽  
Vol 2012 ◽  
pp. 1-19 ◽  
Author(s):  
David W. Zhang ◽  
Juan B. Rodríguez-Molina ◽  
Joshua R. Tietjen ◽  
Corey M. Nemec ◽  
Aseem Z. Ansari

The C-terminal domain (CTD) of RNA polymerase II (Pol II) consists of conserved heptapeptide repeats that function as a binding platform for different protein complexes involved in transcription, RNA processing, export, and chromatin remodeling. The CTD repeats are subject to sequential waves of posttranslational modifications during specific stages of the transcription cycle. These patterned modifications have led to the postulation of the “CTD code” hypothesis, where stage-specific patterns define a spatiotemporal code that is recognized by the appropriate interacting partners. Here, we highlight the role of CTD modifications in directing transcription initiation, elongation, and termination. We examine the major readers, writers, and erasers of the CTD code and examine the relevance of describing patterns of posttranslational modifications as a “code.” Finally, we discuss major questions regarding the function of the newly discovered CTD modifications and the fundamental insights into transcription regulation that will necessarily emerge upon addressing those challenges.


2011 ◽  
Vol 31 (6) ◽  
pp. 1288-1300 ◽  
Author(s):  
P. Thebault ◽  
G. Boutin ◽  
W. Bhat ◽  
A. Rufiange ◽  
J. Martens ◽  
...  

1999 ◽  
Vol 274 (32) ◽  
pp. 22127-22130 ◽  
Author(s):  
Rodney J. Moreland ◽  
Franck Tirode ◽  
Qin Yan ◽  
Joan Weliky Conaway ◽  
Jean-Marc Egly ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document