INO80 exchanges H2A.Z for H2A by translocating on DNA proximal to histone dimers.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 28604691.
- Also identified by DOI 10.1038/ncomms15616 and PMC identifier 5472786.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
ATP-dependent chromatin remodellers modulate nucleosome dynamics by mobilizing or disassembling nucleosomes, as well as altering nucleosome composition. These chromatin remodellers generally function by translocating along nucleosomal DNA at the H3-H4 interface of nucleosomes. Here we show that, unlike other remodellers, INO80 translocates along DNA at the H2A-H2B interface of nucleosomes and persistently displaces DNA from the surface of H2A-H2B. DNA translocation and DNA torsional strain created near the entry site of nucleosomes by INO80 promotes both the mobilization of nucleosomes and the selective exchange of H2A.Z-H2B dimers out of nucleosomes and replacement by H2A-H2B dimers without any additional histone chaperones. We find that INO80 translocates and mobilizes H2A.Z-containing nucleosomes more efficiently than those containing H2A, partially accounting for the preference of INO80 to replace H2A.Z with H2A. Our data suggest that INO80 has a mechanism for dimer exchange that is distinct from other chromatin remodellers including its paralogue SWR1.
Medical subject headings
- Adenosine Triphosphatases
- Chromatin Assembly and Disassembly
- DNA, Fungal
- Histones
- Saccharomyces cerevisiae
- Saccharomyces cerevisiae Proteins