Nuclear actin and myosin I are required for RNA polymerase I transcription

2004 ◽  
Vol 6 (12) ◽  
pp. 1165-1172 ◽  
Author(s):  
Vlada V. Philimonenko ◽  
Jian Zhao ◽  
Sebastian Iben ◽  
Hana Dingová ◽  
Katarína Kyselá ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase I ◽  
Nuclear Actin ◽  
Myosin I ◽  
Polymerase I

scholarly journals Nuclear myosin I acts in concert with polymeric actin to drive RNA polymerase I transcription

2008 ◽  
Vol 22 (3) ◽  
pp. 322-330 ◽  
Author(s):  
J. Ye ◽  
J. Zhao ◽  
U. Hoffmann-Rohrer ◽  
I. Grummt
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase I ◽  
Myosin I ◽  
Nuclear Myosin I ◽  
Polymerase I ◽  
Polymeric Actin

scholarly journals β-Actin and Nuclear Myosin I are responsible for nucleolar reorganization during DNA Repair

2019 ◽  
Author(s):  
Elena Cerutti ◽  
Laurianne Daniel ◽  
Lise-Marie Donnio ◽  
Damien Neuillet ◽  
Charlene Magnani ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Repair ◽  
Rna Polymerase ◽  
Ribosomal Dna ◽  
Rna Polymerase I ◽  
Dna And Rna ◽  
Beta Actin ◽  
Myosin I ◽  
Nuclear Myosin I ◽  
Polymerase I

AbstractDuring DNA Repair, ribosomal DNA and RNA polymerase I (rDNA/RNAP1) are reorganized within the nucleolus. Until now, the proteins and the molecular mechanism governing this reorganisation remained unknown.Here we show that Nuclear Myosin I (NMI) and Nuclear Beta Actin (ACTβ) are essential for the proper reorganisation of the nucleolus, after completion of the DNA Repair reaction.In NMI and ACTβ depleted cells, the rDNA/RNAP1 complex can be displaced at the periphery of the nucleolus after DNA damage but cannot re-enter within the nucleolus after completion of the DNA Repair. Both proteins act concertedly in this process. NMI binds the damaged rDNA at the periphery of the nucleolus, while ACTβ brings the rDNA back within the nucleolus after DNA repair completion. Our results reveal a previously unidentified function for NMI and ACTβ and disclose how these two proteins work in coordination to re-establish the proper rDNA position after DNA repair.

scholarly journals As functional nuclear actin comes into view, is it globular, filamentous, or both?

2008 ◽  
Vol 180 (6) ◽  
pp. 1061-1064 ◽  
Author(s):  
Thoru Pederson
Keyword(s):  
Signal Transduction ◽  
Rna Polymerase ◽  
Research Field ◽  
Rna Polymerases ◽  
Rna Polymerase I ◽  
Nuclear Actin ◽  
Structural Form ◽  
Rapid Transition ◽  
Polymerase I ◽  
Polymeric Actin

The idea that actin may have an important function in the nucleus has undergone a rapid transition from one greeted with skepticism to a now rapidly advancing research field. Actin has now been implicated in transcription by all three RNA polymerases, but the structural form it adopts in these processes remains unclear. Recently, a claim was made that monomeric nuclear actin plays a role in signal transduction, while a just-published study of RNA polymerase I transcription has implicated polymeric actin, consorting with an isoform of its classical partner myosin. Both studies are critically discussed here, and although there are several issues to be resolved, it now seems reasonable to start thinking about functions for both monomeric and assembled actin in the nucleus.

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