The Chromodomains of the Chd1 Chromatin Remodeler Regulate DNA Access to the ATPase Motor

Journal Article · Fri Jan 01 04:00:00 EST 2010 · Molecular Cell

DOI:https://doi.org/10.1016/j.molcel.2010.08.012· OSTI ID:1019963

Hauk, G; McKnight, J; Nodelman, I; Bowman, G

Chromatin remodelers are ATP-driven machines that assemble, slide, and remove nucleosomes from DNA, but how the ATPase motors of remodelers are regulated is poorly understood. Here we show that the double chromodomain unit of the Chd1 remodeler blocks DNA binding and activation of the ATPase motor in the absence of nucleosome substrates. The Chd1 crystal structure reveals that an acidic helix joining the chromodomains can pack against a DNA-binding surface of the ATPase motor. Disruption of the chromodomain-ATPase interface prevents discrimination between nucleosomes and naked DNA and reduces the reliance on the histone H4 tail for nucleosome sliding. We propose that the chromodomains allow Chd1 to distinguish between nucleosomes and naked DNA by physically gating access to the ATPase motor, and we hypothesize that related ATPase motors may employ a similar strategy to discriminate among DNA-containing substrates.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: DOE - OFFICE OF SCIENCE
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 1019963
• Report Number(s): BNL--95809-2011-JA
• Journal Information: Molecular Cell, Journal Name: Molecular Cell Journal Issue: 5 Vol. 39; ISSN 1097-2765
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS
CHROMATIN
CRYSTAL STRUCTURE
DNA
HISTONES
MOTORS
NUCLEOSOMES
SUBSTRATES
national synchrotron light source