Department of Chemistry and Biochemistry
Seminar Announcement
October 22, 2015
Room 114 Smith Hall, 12:30 p.m.*
Dr. Jeffrey Hayes
University of Rochester Medical Center
Department of Biochemistry and Biophysics
Macromolecular Interactions of Core and Linker Histone 'tail'
Domains that Control Chromatin Structure and Function
The chromosomes of humans and other eukaryotes provide the seemingly contrasting functions of compacting
the genomic DNA several thousand times its length while also allowing for efficient processes such as
replicating the genome and expressing genes encoded within. To accomplish this, the DNA is assembled into a
complicated, multifaceted complex known as chromatin. The initial level of packaging DNA into chromatin
involves wrapping short ~200 bp segments around protein spools comprised of the core histone proteins into
structures known as nucleosomes. Immensely long, genome-sized strings of nucleosomes are assembled into a
hierarchy of higher-order chromatin structures, to form chromosomes. Formation of such higher-order involves
essential inter-nucleosome interactions provided by the ‘tail’ domains of the core histone proteins, which
protrude out from the main body of nucleosomes. Posttranslational modification within these domains is a key
component in the regulation of gene expression. While nucleosome structure is fairly well understood, higherorder chromatin structures and inter-nucleosome interactions remain poorly defined. Moreover, how
posttranslational modifications within the tail domains result in modulation of chromatin higher order structures
to regulate gene expression is not well understood. Using site-directed crosslinking, we have defined intra- and
inter-nucleosome interactions for core histone tail domains and how an additional chromatin component, linker
histone H1, affects these contacts. In addition, using biochemical and fluorescence techniques, we have defined
the COOH-terminal domain (CTD) of linker histones as an intrinsically disordered domain and shown that the
CTD adopts defined structure(s) upon H1 binding to nucleosomes.
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Kan, P.-Y., Lu, X, Hansen, J.C. and Hayes, J.J. (2007). The H3 tail domain participates in multiple interactions during folding and selfassociation of nucleosome arrays. Mol. Cell. Biol. 27, 2084-2091.
Wang, X, and Hayes, J.J. (2008). Acetylation mimics within individual core histone tail domains indicate distinct roles in regulating stability of
higher-order chromatin structure. Mol. Cell. Biol. 21, 227–236.
Kan, P.-Y., Caterino, T., and Hayes, J.J. (2009) 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. 29, 538-546.
Caterino, T.L., Fang, H., and Hayes, J.J. (2011). Nucleosome Linker DNA Contacts and Induces Specific Folding of the Intrinsically Disordered
H1 Carboxyl Terminal Domain. Mol. Cell Biol. 31:2341-2348. PMID: 21464206.
Fang, H., Clark, D.J., Hayes, J.J. (2012). DNA and nucleosomes direct distinct folding of a linker histone H1 C-terminal domain. Nuc. Acids
Res. 40:1475-1484 PMID: 22021384. PMC3287190
*Pre-seminar social time – 12:15 p.m. A pizza lunch with the speaker will follow after the presentation in the
Smith Hall student lounge.