QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Supplemental Research Data All Versions of this Article: gad.455908v1 22/3/322    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Ye, J. Articles by Grummt, I. Search for Related Content PubMed PubMed Citation Articles by Ye, J. Articles by Grummt, I. Social Bookmarking                   What's this?

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

Division of Molecular Biology of the Cell II, German Cancer Research Center, D-69120 Heidelberg, Germany

Actin is associated with all three nuclear RNA polymerases and acts in concert with nuclear myosin I (NM1) to drive transcription. Practically nothing is known regarding the state of actin and the functional interplay of actin and NM1 in transcription. Here we show that actin and NM1 act in concert to promote RNA polymerase I (Pol I) transcription. Drugs that prevent actin polymerization or inhibit myosin function inhibit Pol I transcription in vivo and in vitro. Mutants that stabilize the polymeric state actin are tightly associated with Pol I and activate transcription, whereas a polymerization-deficient mutant does not bind to Pol I and does not promote rDNA transcription. Consistent with nuclear actin and myosin synergizing in transcription activation, NM1 mutants that lack specific functions, such as binding to ATP, actin, or calmodulin, are incapable of associating with Pol I and rDNA. The results show that actin polymerization and the motor function of NM1 are required for association with the Pol I transcription machinery and transcription activation. These observations provide insights into the cooperative action of actin and myosin in the nucleus and reveal an actomyosin-based mechanism in transcription.

[Keywords: RNA polymerase I; nuclear myosin; actin; transcription; cofilin]]

Received September 4, 2007; revised version accepted November 28, 2007.

E-MAIL I.Grummt{at}DKFZ.de; FAX 49-6221-423467.

Supplemental material is available at http://www.genesdev.org.

Article published online ahead of print. Article and publication date are online at http://www.genesdev.org/cgi/doi/10.1101/gad.455908

CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				T. Pederson As functional nuclear actin comes into view, is it globular, filamentous, or both? J. Cell Biol., March 24, 2008; 180(6): 1061 - 1064. [Abstract] [Full Text] [PDF]