ISWI remodelers slide nucleosomes with coordinated multi-base-pair entry steps and single-base-pair exit steps.
ISWI remodelers slide nucleosomes with coordinated multi-base-pair entry steps and single-base-pair exit steps.
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DOI：
10.1016/j.cell.2012.12.040
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发表时间：
2013-01-31
期刊：
影响因子：
64.5
通讯作者：
Zhuang X
中科院分区：
文献类型：
--
作者：
Deindl S;Hwang WL;Hota SK;Blosser TR;Prasad P;Bartholomew B;Zhuang X
ISWI-family enzymes remodel chromatin by sliding nucleosomes along DNA, but the nucleosome translocation mechanism remains unclear. Here we use single-molecule FRET to probe nucleosome translocation by ISWI-family remodelers. Distinct ISWI-family members translocate nucleosomes with a similar stepping pattern maintained by the catalytic subunit of the enzyme. Nucleosome remodeling begins with a 7-bp step of DNA translocation followed by 3-bp subsequent steps towards the exit side of nucleosomes. These multi-bp, compound steps are comprised of 1-bp substeps. DNA movement on the entry side of the nucleosome occurs only after 7 bp of exit-side translocation and each entry-side step draws in a 3-bp equivalent of DNA that allows three additional base pairs to be moved to the exit side. Our results suggest a remodeling mechanism with precise coordination at different nucleosomal sites featuring DNA translocation towards the exit side in 1-bp steps preceding multi-bp steps of DNA movement on the entry side.
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