News and Views
Nature Structural & Molecular Biology 15, 432 - 433 (2008)
doi:10.1038/nsmb0508-432
New clues to actin function in chromatin regulation
Aaron J Gottschalk1, Ronald C Conaway1 & Joan Weliky Conaway1
-
Aaron J. Gottschalk, Ronald C. Conaway and Joan Weliky Conaway are at the Stowers Institute for Medical Research, Kansas City, Missouri 64110, USA, and the Department of Biochemistry and Molecular Biology, Kansas University Medical Center, Kansas City, Kansas 66160, USA.
e-mail: jlc@stowers-institute.org
Abstract
Since the discovery that actin and actin-related proteins (ARPs) reside in the nucleus as integral subunits of chromatin-modifying and chromatin-remodeling complexes, efforts to uncover their roles in chromatin regulation have met with limited success. In a new study, the previously mysterious helicase-SANT–associated (HSA) domain found in many chromatin regulatory complexes is shown to act as a module that directs recruitment and contributes to the action of actin and ARPs in chromatin regulation.
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
RESEARCH
The HSA domain binds nuclear actin-related proteins to regulate chromatin-remodeling ATPasesNature Structural & Molecular Biology Article (01 May 2008)
The nuclear actin-related proteins Arp7 and Arp9: a dimeric module that cooperates with architectural proteins for chromatin remodelingThe EMBO Journal Article (16 Jun 2003)
The nuclear actin-related proteins Arp7 and Arp9: a dimeric module that cooperates with architectural proteins for chromatin remodelingThe EMBO Journal Article (16 Jun 2003)
Swi3p controls SWI/SNF assembly and ATP-dependent H2A-H2B displacementNature Structural & Molecular Biology Article (01 Jun 2007)
See all 13 matches for Research