Graduate Program Information
My Contact Information

Professor of Biochemistry and Biophysics
Ph.D. Johns Hopkins University 1990

Each eukaryotic cell must execute a complex program of specific gene expression. The DNA of the genome is intimately complexed with proteins into an assembly known as chromatin. Compaction and storage of genomic DNA has long been viewed as the main function of this assembly; however, recent work has demonstrated that in some instances, chromatin structure play an important role in bringing about this pattern of specific expression, and it is likely that the structural elements of chromatin have been integrated into many transcriptional control mechanisms.

The goal of the research in this laboratory is to provide detailed structure information on the protein-DNA interactions and DNA organization within chromatin, and to correlate this information with simple functional assays of the consequences of this organization. Model chromatin complexes will be prepared in vitro and structurally analyzed with chemical approaches. In addition, cloning expression of histone proteins with specific mutations will be useful in the determination of relevant domains within these proteins while facilitating the creation of site-specific probes of protein and DNA structure with chromatin.

Visit my Lab Page  
 
 

Recent Publications

Thiriet C, Hayes JJ (2008) Linker histone phosphorylation regulates global timing of replication origin firing. J Biol Chem,

Kan PY, Caterino TL, Hayes JJ (2008) The H4 tail domain participates in intra- and inter-nucleosome interactions with protein and DNA during folding and oligomerization of nucleosome arrays. Mol Cell Biol,

Wang X, Hayes JJ (2008) Acetylation mimics within individual core histone tail domains indicate distinct roles in regulating the stability of higher-order chromatin structure. Mol Cell Biol, 28:227-36

Yang Z, Zheng C, Hayes JJ (2007) The core histone tail domains contribute to sequence-dependent nucleosome positioning. J Biol Chem, 282:7930-8

Kan PY, Hayes JJ (2007) Detection of interactions between nucleosome arrays mediated by specific core histone tail domains. Methods, 41:278-85

Kan PY, Lu X, Hansen JC, Hayes JJ (2007) The H3 tail domain participates in multiple interactions during folding and self-association of nucleosome arrays. Mol Cell Biol, 27:2084-91

Wang X, Hayes JJ (2007) Site-specific binding affinities within the H2B tail domain indicate specific effects of lysine acetylation. J Biol Chem,

Wang X, Hayes JJ (2006) Physical methods used to study core histone tail structures and interactions in solution. Biochem Cell Biol, 84:578-88

Jagannathan I, Cole HA, Hayes JJ (2006) Base excision repair in nucleosome substrates. Chromosome Res, 14:27-37

Thiriet C, Hayes JJ (2006) Histone dynamics during transcription: exchange of H2A/H2B dimers and H3/H4 tetramers during pol II elongation. Results Probl Cell Differ, 41:77-90

Zheng C, Lu X, Hansen JC, Hayes JJ (2005) Salt-dependent intra- and internucleosomal interactions of the H3 tail domain in a model oligonucleosomal array. J Biol Chem, 280:33552-7

Thiriet C, Hayes JJ (2005) Replication-independent core histone dynamics at transcriptionally active loci in vivo. Genes Dev, 19:677-82

Thiriet C, Hayes JJ (2005) Chromatin in need of a fix: phosphorylation of H2AX connects chromatin to DNA repair. Mol Cell, 18:617-22

Yang Z, Zheng C, Thiriet C, Hayes JJ (2005) The core histone N-terminal tail domains negatively regulate binding of transcription factor IIIA to a nucleosome containing a 5S RNA gene via a novel mechanism. Mol Cell Biol, 25:241-9

Owen BA, Yang Z, Lai M, Gajek M, Badger JD2nd, Hayes JJ, Edelmann W, Kucherlapati R, Wilson TM, McMurray CT (2005) (CAG)(n)-hairpin DNA binds to Msh2-Msh3 and changes properties of mismatch recognition. Nat Struct Mol Biol, 12:663-70

Hayes JJ (2004) In vitro analysis of chromatin structure in model systems. Methods, 33:1-2

Yang Z, Hayes JJ (2004) Large scale preparation of nucleosomes containing site-specifically chemically modified histones lacking the core histone tail domains. Methods, 33:25-32

Vitolo JM, Yang Z, Basavappa R, Hayes JJ (2004) Structural Features of Transcription Factor IIIA Bound to a Nucleosome in Solution. Mol Cell Biol, 24:697-707

Zheng C, Hayes JJ (2004) Probing core histone tail-DNA interactions in a model dinucleosome system. Methods Enzymol, 375:179-93

Graduate students in my laboratory work toward a Ph.D. degree in the following program[s]:

Ph.D. in Biochemistry
Ph.D. in Biophysics

Ph.D. candidates in my laboratory may also be affiliated with these programs:

Contact Information

E-Mail: jeffrey_hayes@urmc.rochester.edu

Jeffrey J. Hayes
Department of Biochemistry and Biophysics
University of Rochester School of Medicine and Dentistry
601 Elmwood Ave, Box 712
Rochester, New York 14642

Office: Medical Center 3-6710
Telephone: (585) 275-1706; Fax: (585) 275-6007