This domain appears to play a crucial role in chromatin remodelling for yeast SWI/SNF. It binds histones. It is required for mobilising nucleosomes and lies within the catalytic subunit of the yeast SWI/SNF. It is found to be universally conserved PMID:21835776.
This domain lies within the catalytic subunit (Snf2) of the yeast SWI/SNF chromatin remodelling complex. It binds histones and is required for mobilising nucleosomes [ (PUBMED:21835776) ]. This domain is conserved and can also be found in Snf2 homologues, such as Sth1 [ (PUBMED:9799253) ].
A new, highly conserved domain in Swi2/Snf2 is required for SWI/SNF remodeling.
Nucleic Acids Res. 2011; 39: 9155-66
Display abstract
SWI/SNF is an ATP-dependent remodeler that mobilizes nucleosomes and hasimportant roles in gene regulation. The catalytic subunit of SWI/SNF has anATP-dependent DNA translocase domain that is essential for remodeling. Besidesthe DNA translocase domain there are other domains in the catalytic subunit ofSWI/SNF that have important roles in mobilizing nucleosomes. One of thesedomains, termed SnAC (Snf2 ATP Coupling), is conserved in all eukaryotic SWI/SNF complexes and is located between the ATPase and A-T hook domains. Here, we showthat the SnAC domain is essential for SWI/SNF activity. The SnAC domain is notrequired for SWI/SNF complex integrity, efficient nucleosome binding, orrecruitment by acidic transcription activators. The SnAC domain is howeverrequired in vivo for transcription regulation by SWI/SNF as seen by alternativecarbon source growth assays, northern analysis, and genome-wide expressionprofiling. The ATPase and nucleosome mobilizing activities of SWI/SNF areseverely affected when the SnAC domain is removed or mutated. The SnAC domainpositively regulates the catalytic activity of the ATPase domain of SWI/SNF tohydrolyze ATP without significantly affecting its affinity for ATP.
