Three-dimensional structure of human chromatin accessibility complex hCHRAC by electron microscopy

Journal Article · Mon Dec 01 04:00:00 EST 2008 · Journal of Structural Biology

DOI:https://doi.org/10.1016/j.jsb.2008.08.007· OSTI ID:1040040

Hu, M; Hainfeld, J; Zhang, Y -B; Qian, L; Brinas, R P; Kuznetsova, L

ATP-dependent chromatin remodeling complexes modulate the dynamic assembly and remodeling of chromatin involved in DNA transcription, replication, and repair. There is little structural detail known about these important multiple-subunit enzymes that catalyze chromatin remodeling processes. Here we report a three-dimensional structure of the human chromatin accessibility complex, hCHRAC, using single particle reconstruction by negative stain electron microscopy. This structure shows an asymmetric 15 x 10 x 12 nm disk shape with several lobes protruding out of its surfaces. Based on the factors of larger contact area, smaller steric hindrance, and direct involvement of hCHRAC in interactions with the nucleosome, we propose that four lobes on one side form a multiple-site contact surface 10 nm in diameter for nucleosome binding. This work provides the first determination of the three-dimensional structure of the ISWI-family of chromatin remodeling complexes.

• Research Organization: BROOKHAVEN NATIONAL LABORATORY (BNL)
• Sponsoring Organization: LABORATORY-DIRECTED RESEARCH AND DEVELOPMENT
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 1040040
• Report Number(s): BNL--90060-2008-JA; YN0100000
• Journal Information: Journal of Structural Biology, Journal Name: Journal of Structural Biology Journal Issue: 3 Vol. 164; ISSN JSBIEM; ISSN 1047-8477
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
60 APPLIED LIFE SCIENCES
CHROMATIN
DNA
ELECTRON MICROSCOPY
ENZYMES
NUCLEOSOMES
REPAIR
SHAPE
STAINS
TRANSCRIPTION
chromatin remodeling
electron microscopy
hCHRAC
nucleosome
three-dimensional structure