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Erin Green

Asst Prof

Biological Sciences
Biological Sciences, Room 325
Phone
410-455-1189
egreen@umbc.edu
Education
Stanford University (2013)
Ph D, University of California, Berkeley (2007)
BA, Bryn Mawr College (2000)
Website
Research 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.

Selected Classes
Fall 2016 BIOL 303 – Cell Biology
Fall 2015 BIOL 426 – Appr To Molecular Biol
Intellectual Contributions

The histone methyltransferases Set5 and Set1 have overlapping functions in gene silencing and telomere maintenance. 2 vol. 12 93-104 Epigenetics

Choose Your Own Adventure: The Role of Histone Modifications in Yeast Cell Fate. Journal of molecular biology

Set5 and Set1 cooperate to repress gene expression at telomeres and retrotransposons. 4 vol. 9 Epigenetics

Proteome-wide enrichment of proteins modified by lysine methylation. 1 vol. 9 37-50 Nature protocols

New marks on the block: Set5 methylates H4 lysines 5, 8 and 12. 4 vol. 3 335-9 Nucleus (Austin, Tex.)

A negative feedback loop at the nuclear periphery regulates GAL gene expression. 7 vol. 23 1367-75 Molecular biology of the cell

Methylation of H4 lysines 5, 8 and 12 by yeast Set5 calibrates chromatin stress responses. 3 vol. 19 361-3 Nature structural & molecular biology

Overlapping regulation of CenH3 localization and histone H3 turnover by CAF-1 and HIR proteins in Saccharomyces cerevisiae. 1 vol. 187 9-19 Genetics

Members of the H3K4 trimethylation complex regulate lifespan in a germline-dependent manner in C. elegans. 7304 vol. 466 383-7 Nature

Replication-independent histone deposition by the HIR complex and Asf1. 22 vol. 15 2044-9 Current biology : CB