A SWI/SNF-family chromatin remodeling subcomplex from yeast is identified (RSC1) that is specialized to slide nucleosomes residing on DNA sequences that confer partial nucleosome unwrapping, with assistance from accessory factors.

A combination of genetics, expression, genomic localization, and genomic nucleosome profiling demonstrates antagonism between two chromatin remodelers that reveal different mechanisms at different promoter architectures.

Single-particle imaging of RSC and ISW2 chromatin remodelers on DNA stretched between dual optical tweezers reveals distinctive 1D diffusion and opposing push–pull nucleosome translocation on engagement with sparse nucleosome arrays.

In vitro single-particle tracking reveals that ATP binding increases the one-dimensional diffusion of yeast chromatin remodeler SWR1 on DNA stretched between optical tweezers and diffusion is confined by protein roadblocks and nucleosomes.

The chromatin remodeller BRG1 is recruited to pluripotency-associated gene regulatory elements by the pioneer transcription factor OCT4 to support further transcription factor binding and gene regulation.

The ATP-dependent chromatin remodeler Chd1 controls nucleosome turnover to allow RNA Polymerase to transcribe in vivo.

The structure of the chromatin remodeller CHD4 bound to a nucleosome reveals differences to the known Chd1-nucleosome complex and maps cancer mutations.

Auto-inhibition of ISWI-family ATP-dependent chromatin remodelers is relieved by a conserved feature of the nucleosome.

Unlike Chd1, ISWI remodelers preferentially shift asymmetric nucleosomes toward the side possessing a wild type acidic patch, regardless of DNA lengths flanking the nucleosome.

Chromatin remodeling enzymes perform target search by utilizing ATP-binding and hydrolysis to facilitate 1D-diffusion on and rapid detachment from chromatin in living yeast.