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Published online on March 13, 2007, 10.1073/pnas.0700706104
PNAS | March 20, 2007 | vol. 104 | no. 12 | 4913-4918
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BIOLOGICAL SCIENCES / BIOPHYSICS
Conformational flexibility in the chromatin remodeler RSC observed by electron microscopy and the orthogonal tilt reconstruction method

Andres E. Leschziner*,{dagger}, Anjanabha Saha{ddagger},§, Jacqueline Wittmeyer{ddagger}, Yongli Zhang, Carlos Bustamante*,{dagger},¶,||,**,{dagger}{dagger}, Bradley R. Cairns{dagger},{ddagger},§, and Eva Nogales*,{dagger},¶,{dagger}{dagger}

Departments of *Molecular and Cell Biology, ||Chemistry, and **Physics, and {dagger}{dagger}Howard Hughes Medical Institute, University of California, Berkeley, CA 94720; {ddagger}Department of Oncological Sciences, Huntsman Cancer Institute, and §Howard Hughes Medical Institute, University of Utah School of Medicine, Salt Lake City, UT 84112; and Lawrence Berkeley National Laboratory, Berkeley, CA 94720

Contributed by Carlos Bustamante, January 25, 2007 (received for review January 12, 2007)

Chromatin remodeling complexes (remodelers) are large, multisubunit macromolecular assemblies that use ATP hydrolysis to alter the structure and positioning of nucleosomes. The mechanisms proposed for remodeler action on nucleosomes are diverse, and require structural evaluation and insights. Previous reconstructions of remodelers using electron microscopy revealed interesting features, but also significant discrepancies, prompting new approaches. Here, we use the orthogonal tilt reconstruction method, which is well suited for heterogeneous samples, to provide a reconstruction of the yeast RSC (remodel the structure of chromatin) complex. Two interesting features are revealed: first, we observe a deep central cavity within RSC, displaying a remarkable surface complementarity for the nucleosome. Second, we are able to visualize two distinct RSC conformers, revealing a major conformational change in a large protein "arm," which may shift to further envelop the nucleosome. We present a model of the RSC-nucleosome complex that rationalizes the single molecule results obtained by using optical tweezers and also discuss the mechanistic implications of our structures.

chromatin remodeling | single particle electron microscopy

Freely available online through the PNAS open access option.

Author contributions: A.E.L., C.B., B.R.C., and E.N. designed research; A.E.L., A.S., J.W., and Y.Z. performed research; A.E.L. contributed new reagents/analytic tools; A.E.L., C.B., B.R.C., and E.N. analyzed data; and A.E.L., C.B., B.R.C., and E.N. wrote the paper.

The authors declare no conflict of interest.

This article contains supporting information online at www.pnas.org/cgi/content/full/0700706104/DC1.

{dagger}To whom correspondence may be addressed. E-mail: aeleschziner{at}berkeley.edu, carlos{at}alice.berkeley.edu, brad.cairns{at}hci.utah.edu, or enogales{at}lbl.gov

© 2007 by The National Academy of Sciences of the USA


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