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Erin Green, Ph.D.

Assistant Professor

DSC_5296

Office: BS 324
Phone: 410-455-1189
Lab: BS 353, 354, 359
Lab Phone: 410-455-2248
Email:  egreen@umbc.edu
Lab Website: greenlab.umbc.edu

Education

Postdoctoral, Stanford University, 2013

Ph.D., University of California, Berkeley, 2007

 

Professional Interests

Research in our lab aims to understand how post-translational modifications of proteins direct epigenetic and cellular signaling pathways to regulate key biological functions, including the establishment of proper states of gene expression and the ability of cells to respond to stress.  Histones, the primary protein component of chromatin, are subject to many types of post-translational modification, including acetylation, phosphorylation and methylation. These modifications are critical to controlling the accessibility of DNA during essential processes such as transcription and DNA repair.

We are specifically interested in methylation of histone lysine residues, a modification system that has been well-established to regulate chromatin structure and function. Aberrant regulation of histone lysine methylation leads to the disruption of chromatin homeostasis and has been implicated in numerous human pathologies, including tumorigenesis.  There remain many unanswered questions regarding the functional and mechanistic details of both canonical and novel sites of histone methylation.  Additionally, the existence of non-histone protein methylation is emerging as a key regulator of nuclear signaling pathways, but the extent and function of these methylation events are largely unknown.

Our primary research objectives are to (1) identify new mechanisms of chromatin regulation mediated by novel histone methylation events and (2) develop a comprehensive understanding of lysine methylation as a broad regulator of nuclear signaling pathways. We use budding yeast as a model system, integrating molecular biology, genetics, biochemistry, genomics and proteomics.  The evolutionary conservation of many of the players involved in lysine methylation signaling allows our work to be broadly applicable to higher eukaryotes, and will provide insight in to the role of these factors in diverse human diseases.

 

Publications

Martin, G.M.*, King, D.A.*, Green, E.M.*, Garcia-Nieto, P.E., Alexander, R., Collins, S.R., Krogan, N.J., Gozani, O.P. and A.J. Morrison. Set5 and Set1 cooperate to repress gene expression at telomeres and retrotransposons. Epigenetics 9: 513-22, 2014.

Abstract: http://www.ncbi.nlm.nih.gov/pubmed/24442241

Carlson, S.M.*, Moore, K.E.*, Green, E.M., Mas Martin, G., and O. Gozani. Proteome-wide enrichment of proteins modified by lysine methylation. Nat. Protoc. 9: 37-50, 2014.

Abstract: http://www.ncbi.nlm.nih.gov/pubmed/24309976

Green, E.M., Morrison, A.J. and O. Gozani.  New marks on the block: Set5 methylates H4 lysines 5, 8 and 12. Nucleus 3: 335-9, 2012.

Abstract: http://www.ncbi.nlm.nih.gov/pubmed/22688645

Green, E.M.*, Mas, G.,* Young, N.L., Garcia, B.A. and O. Gozani.  Methylation of H4 lysines 5, 8 and 12 by yeast Set5 calibrates chromatin stress responses. Nat. Struct. Mol. Biol. 19: 361-3, 2012.

Abstract: http://www.ncbi.nlm.nih.gov/pubmed/22343720

Green, E.M. and O. Gozani.  Everybody’s welcome: The big tent approach to epigenetic drug discovery.  Drug Discov. Today Ther. Strateg., 9: e75-e81, 2012.

Abstract: http://www.ncbi.nlm.nih.gov/pubmed/23505394

Greer, E.L., Maures, T.J., Hauswirth A.G., Green, E.M., Leeman, D.S., Maro, G.S., Han, S., Banko, M.R., Gozani, O. and A. Brunet. Members of the H3K4 trimethylation complex regulate lifespan in a germline-dependent manner in C. elegans. Nature 466: 383-7, 2010.

Abstract: http://www.ncbi.nlm.nih.gov/pubmed/20555324

Green, E.M.*, Jiang, Y.*, Joyner, R., and K. Weis.  A negative feedback loop at the nuclear periphery regulates GAL gene expression. Mol. Biol. Cell 7: 1367-75, 2012.

Abstract: http://www.ncbi.nlm.nih.gov/pubmed/22323286

Lopes da Rosa, J.*, Holik, J.*, Green, E.M.*, Rando, O. and P.D. Kaufman.  Overlapping regulation of CenH3 localization and histone H3 turnover by CAF-1 and HIR proteins in Saccharomyces cerevisiae. Genetics 187: 9-19, 2011.

Abstract: http://www.ncbi.nlm.nih.gov/pubmed/20944015

Green, E.M., Antczak, A.A., Bailey, A.O., Franco, A.A., Wu, K., Yates, J.R. 3rd and P.D. Kaufman.  Replication-independent histone deposition by the HIR complex and Asf1. Curr. Biol., 15: 2044-9, 2005.

Abstract: http://www.ncbi.nlm.nih.gov/pubmed/16303565

 

*These authors contributed equally to the work.