Jeffrey Joseph Hayes, Ph.D.

See information for Patients. Viewing information for Researchers.

Contact

University of Rochester
School of Medicine and Dentistry
601 Elmwood Ave, Box 712
Rochester, New York 14642

Office: 585 275-1706

Fax: 585 275-6007

Portrait

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.

Current Appointments

Education
PhD Chemistry Johns Hopkins University 1990
MS Chemistry Bowling Green University 1986
BS Chemistry Bowling Green University 1983

Lab Website

http://dbb.urmc.rochester.edu/labs/hayes/index.htm

Recent Journal Articles
Showing the 5 most recent journal articles. (88 available)
Kan, P. Y.; Caterino, T. L.; Hayes, J. J.;. "The H4 tail domain participates in intra- and internucleosome interactions with protein and DNA during folding and oligomerization of nucleosome arrays". Mol Cell Biol 29 (2009): 538-46.
Thiriet, C.; Hayes, J. J.;. "Linker histone phosphorylation regulates global timing of replication origin firing". J Biol Chem 284 (2009): 2823-9.
Wang, X.; Hayes, J. J.;. "Acetylation mimics within individual core histone tail domains indicate distinct roles in regulating the stability of higher-order chromatin structure". Mol Cell Biol 28 (2008): 227-36.
Wang, X.; Hayes, J. J.;. "Site-specific binding affinities within the H2B tail domain indicate specific effects of lysine acetylation". J Biol Chem (2007).
Yang Z; Zheng C; Hayes JJ. "The core histone tail domains contribute to sequence-dependent nucleosome positioning." The Journal of biological chemistry. 2007; 282(11):7930-8. Epub 2007 Jan 17.