Structure-function analysis of SWI2/SNF2 enzymes
- PMID: 16793413
- DOI: 10.1016/S0076-6879(05)09022-1
Structure-function analysis of SWI2/SNF2 enzymes
Abstract
Biochemical and structural progress over the last years has revealed that SWI2/SNF2 family chromatin remodeling or DNA repair enzymes are molecular motors that transport duplex DNA along a helicase-like domain using ATP-hydrolysis. The screw motion of DNA along the active site probably generates the force to disrupt chromatin or other protein:DNA complexes. In this chapter, we describe biochemical and structural approaches to study the molecular mechanism of SWI2/SNF2 enzymes. In particular, we describe assays to monitor DNA dependent ATPase activity, translocation on duplex DNA, and DNA distortion activity. We also describe recent progress in the crystallization and structure determination of SWI2/SNF2 enzymes in complex with duplex DNA.
Similar articles
-
X-ray structures of the Sulfolobus solfataricus SWI2/SNF2 ATPase core and its complex with DNA.Cell. 2005 May 6;121(3):363-73. doi: 10.1016/j.cell.2005.03.026. Cell. 2005. PMID: 15882619
-
Snf2 family ATPases and DExx box helicases: differences and unifying concepts from high-resolution crystal structures.Nucleic Acids Res. 2006;34(15):4160-7. doi: 10.1093/nar/gkl540. Epub 2006 Aug 25. Nucleic Acids Res. 2006. PMID: 16935875 Free PMC article. Review.
-
Structure of the SWI2/SNF2 chromatin-remodeling domain of eukaryotic Rad54.Nat Struct Mol Biol. 2005 Apr;12(4):350-6. doi: 10.1038/nsmb919. Epub 2005 Apr 3. Nat Struct Mol Biol. 2005. PMID: 15806108
-
The Swi2/Snf2 bromodomain is important for the full binding and remodeling activity of the SWI/SNF complex on H3- and H4-acetylated nucleosomes.Ann N Y Acad Sci. 2008 Sep;1138:366-75. doi: 10.1196/annals.1414.038. Ann N Y Acad Sci. 2008. PMID: 18837912
-
Mechanisms of nucleic acid translocases: lessons from structural biology and single-molecule biophysics.Curr Opin Struct Biol. 2007 Feb;17(1):87-95. doi: 10.1016/j.sbi.2006.11.003. Epub 2006 Dec 6. Curr Opin Struct Biol. 2007. PMID: 17157498 Review.
Cited by
-
Nucleic acid binding activity of human Cockayne syndrome B protein and identification of Ca(2+) as a novel metal cofactor.J Mol Biol. 2009 Sep 4;391(5):820-32. doi: 10.1016/j.jmb.2009.06.078. Epub 2009 Jul 4. J Mol Biol. 2009. PMID: 19580815 Free PMC article.
-
PICKLE is a CHD subfamily II ATP-dependent chromatin remodeling factor.Biochim Biophys Acta. 2013 Feb;1829(2):199-210. doi: 10.1016/j.bbagrm.2012.10.011. Epub 2012 Nov 2. Biochim Biophys Acta. 2013. PMID: 23128324 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases