Christopher L.F. Woodcock

Professor of Biology, University of Massachusetts

Email: chris@bio.umass.edu
C. Woodcock Biology Dept Website

Ph.D.: University College London
Postdoctoral Training: University of Chicago; Harvard University

Structure-Function Relationships in the Nucleus

The eukaryotic nucleus contains several meters of DNA packed into a ~5 micrometer diameter sphere. This DNA must be faithfully replicated each cell cycle, transformed into chromosomes at cell division, and the appropriate genes transcribed at the right times. My work concerns the local and large-scale levels of organization that make these processes possible, bridging the gap between the molecular and cytological approaches to nuclear function.

Based on our work with advanced techniques for examining nuclear organization, we have proposed a novel hypothesis for the mechanism of chromatin folding at the level of the nucleosome that has important implications for transcriptional control. We are actively pursuing this line of enquiry, and also studying the larger scale architecture of chromosomes.

Representative publications:

Fan, Y., Skoultchi, A.I. and Woodcock, C.L. 2006. Role of histone H1 in chromatin structure and function: H1 stoichiometry and nucleosome repeat length. Chromosome Research . In Press.

Horowitz-Scherer, R.A. and Woodcock, C.L. 2006. Organization of chromatin. Chromosoma . In Press.

Fan, Y., Nikitina, T., Zhao, J., Fleury, T.J., Bhattacharyya, R., Bouhassira, E., Stein, A., Woodcock, C.L. , and Skoultchi, A.I. 2005. Depletion of histone H1 in mammals alters global chromatin structure but causes specific changes in gene regulation. Cell , In Press.

Francis, N.J., Kingston, R.E. and Woodcock, C.L. 2004. Chromatin compaction by a Polycomb group protein complex. Science , 306: 1574-1577.

Grigoryev, S.A., Nikitina, T., Pehrson, J., Singh, P., Woodcock, C.L. 2004. Dynamic relocation of epigenetic chromatin markers reveals a dynamic role of constitutive heterochromatin in the transition from proliferation to quiescence. J. Cell Sci. , 117: 6153-6062.

Horowitz-Scherer, R.A. and Woodcock, C.L. 2004. Electron Microscopy of chromatin and chromatin remodeling complexes. Meth. Enzymol. , 376: 29-47.

Nikitina, T. and Woodcock, C.L. 2004. Closed chromatin loops at the ends of chromosomes. J. Cell. Biol. , 166: 161-165.

Smith, C.L., Horowitz-Scherer, R., Flanagan, J.F., Woodcock, C.L. , Peterson, C.L. 2003 Structural analysis of the yeast SWI/SNF chromatin remodeling complex. Nat. Struct. Biol. , 10: 141-5.

Georgel, P.T., Horowitz-Scherer, R.A., Adkins, N., Woodcock, C.L. , Wade, P.A., Hansen, J.C. 2003. Chromatin compaction by human MeCP2. Assembly of novel secondary chromatin structures in the absence of DNA methylation. J. Biol. Chem. , 278: 32181-8.

Fan, Y., Nikitina, T., Morin-Kensicki, E.M., Zhao, J., Magnuson, T.R., Woodcock, C.L. , Skoultchi, A.I. 2003. H1 linker histones are essential for mouse development and affect nucleosome spacing in vivo. Mol. Cell. Biol. , 2003, 23: 4559-72.

Springhetti, E.M., Istomina, N.E., Whisstock, J.C., Nikitina, T., Woodcock, C.L. , Grigoryev, S.A. 2003. Folding and bridging of nucleosome arrays by MENT: the role of the M-loop and the RCL domains. J. Biol. Chem. , 278: 43384-43393.

Woodcock, C. L. and S. Dimitrov (2001). "Higher-order structure of chromatin and chromosomes." Curr Opin Genet Dev 11(2): 130-5.

Bednar, J., V. M. Studitsky, S. A. Grigoryev, G. Felsenfeld and C. L. Woodcock (1999). "The nature of the nucleosomal barrier to transcription: direct observation of paused intermediates by electron cryomicroscopy." Mol Cell 4(3): 377-86.

Bednar, J. and C. L. Woodcock (1999). "Cryoelectron microscopic analysis of nucleosomes and chromatin." Methods Enzymol 304: 191-213.

Grigoryev, S.A., Bednar, J., and Woodcock, C.L. 1999. MENT, a heterochromatin protein that mediates higher order chromatin folding, is a new serpin family member. J. Biol. Chem. 274: 5626-5636.

Bednar, J., Horowitz, R.A., Grigoryev, S. A., Carruthers, L.M., Hansen, J.C., Koster, A.J., and Woodcock, C.L. 1998. Nucleosomes, linder DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin. Proc. Natl. Acad. Sci. 95: 14173-14178.

Grigoryev, S.A. and Woodcock, C.L. 1998. Chromatin structure in granulocytes. A link between tight compaction and accumulation of a heterochromatin-associated protein (MENT). J. Biol. Chem. 273: 3082-3089.

Horowitz, R.A., Koster, A.J., Walz, J., and Woodcock, C.L. 1997. Automated electron microscope tomography of frozen-hydrated chromatin: the irregular three-dimensional zigzag architecture persists in compact, isolated fibers. J. Struct. Biol. 120: 353-362.

Shim, E.Y., Woodcock, C., and Zaret, K.S. 1998. Nucleosome positioning by the winged helix transcription factor HNF3. Genes Dev. 12: 5-10.

Woodcock, C.L. and Horowitz, R.A. 1998. Electron microscopic imaging of chromatin with nucleosome resolution. Methods Cell Biol. 53: 167-186.

Woodcock, C.L. and Horowitz, R.A. 1998. Electron microscopy of chromatin. Methods 12: 84-95.