A new, highly conserved domain in Swi2/Snf2 is required for SWI/SNF remodeling

Payel Sen, Sujana Ghosh, B. Franklin Pugh, Blaine Bartholomew

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

SWI/SNF is an ATP-dependent remodeler that mobilizes nucleosomes and has important roles in gene regulation. The catalytic subunit of SWI/SNF has an ATP-dependent DNA translocase domain that is essential for remodeling. Besides the DNA translocase domain there are other domains in the catalytic subunit of SWI/SNF that have important roles in mobilizing nucleosomes. One of these domains, 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 show that the SnAC domain is essential for SWI/SNF activity. The SnAC domain is not required for SWI/SNF complex integrity, efficient nucleosome binding, or recruitment by acidic transcription activators. The SnAC domain is however required in vivo for transcription regulation by SWI/SNF as seen by alternative carbon source growth assays, northern analysis, and genome-wide expression profiling. The ATPase and nucleosome mobilizing activities of SWI/SNF are severely affected when the SnAC domain is removed or mutated. The SnAC domain positively regulates the catalytic activity of the ATPase domain of SWI/SNF to hydrolyze ATP without significantly affecting its affinity for ATP.

Original languageEnglish (US)
Pages (from-to)9155-9166
Number of pages12
JournalNucleic acids research
Volume39
Issue number21
DOIs
StatePublished - Nov 2011

All Science Journal Classification (ASJC) codes

  • Genetics

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