Chromatin is a nucleoprotein structure, consisting of DNA, histones, and non-histone proteins, which packages DNA in the eukaryotic nucleus. Our research focuses on multi-protein complexes which post-translationally modify histones. We are interested in determining how these complexes are targeted to specific regions of the genome, and the functional consequences of this targeting. We use the budding yeast, Saccharomyces cerevisiae, as a model system due to its well-defined genetic system and the fact that there are a large number of eukaryotic genes that have been evolutionarily conserved between yeast and mammals.
Maltby, V.E., B.J.E. Martin, J.M. Schulze, I. Johnson, T. Hentrich, M.S. Kobor, and L.J. Howe. (2012) Histone H3 Acetylation Negatively Regulates Demethylation of Histone H3K4 by the JmjC Domain Protein, Jhd2. Proc. Nat. Acad. Sci. in press.
Maltby, V.E., B.J.E. Martin, J.M. Schulze, I. Johnson, T. Hentrich, A. Sharma, M.S. Kobor, and L.J. Howe. Histone H3 Lysine 36 Methylation Targets the Isw1b Remodeling Complex to Chromatin. Mol. Cell. Biol. 32:17. (2012)
Chruscicki, A.T., V.E. Macdonald, B.P. Young, C.J. Loewen, and L.J. Howe. Critical Determinants for Chromatin Binding by Saccharomyces cerevisiae Yng1 Exist Outside of the PHD Finger Genetics.185:469-77. (2010)
Choi, J.K., and L.J. Howe. Histone acetylation – truth of consequences? Biochemistry and Cell Biology. 87:139-150.(2009)
MacDonald, V.E. and L.J. Howe. Histone acetylation: where to go and how to get there. Epigenetics. 4:139-143. (2009)
Choi, J.K., D.E. Grimes, K. Rowe, and L.J. Howe. Acetylation of Rsc4p by Gcn5p is essential in the absence of histone H3 acetylation. Mol. Cell. Biol. 28: 6967-6972.(2008)
Shi, X., I. Kachirskaia, K.L. Walter, J.H. Kuo, A. Lake, F. Davrazou, S.M. Chan, D.E.G. Martin, I.M. Fingerman, S.D. Briggs, L.J. Howe, P.J. Utz, T.G.Kutateladze, A.A. Lugovskoy, M.T. Bedford, and O. Gozani. Proteome-wide analysis in Saccharomyces cerevisiae identifies several PHD fingers as novel direct and selective binding modules of histone H3 methylated at either lysine 4 or lysine 36. J. Biol. Chem. 282 :2450-5. (2007)
Martin, D.E.G., K. Baetz, X. Shi, K.L. Walter, V.E. MacDonald, M.J. Wlodarski, O. Gozani, P. Hieter, and L.J. Howe. The Yng1p plant homeodomain finger is a methyl-histone binding module that recognizes lysine 4-methylated histone H3. Mol. Cell. Biol. 26 :7871-9. (2006)
Martin, D.E.G., D.E. Grimes, K. Baetz, and L.J. Howe. Methylation of Histone H3 Mediates the Association of the NuA3 Histone Acetyltransferase with Chromatin. Mol. Cell. Biol. 26: 3018-3028. (2006)