个人简介

GRC Bioorganic Chemistry, Session Chair 2012 Royalty Research Fund 2012 2010 Blavatnik Award nominee from The Rockefeller University 2001Teacher Rated as Excellent, UIUC Center for Teaching Excellence 1999-2001 University of Illinois, Chemical Biology Fellowship 1998 IIT Bombay, silver medal (first in graduating class)

研究领域

Synthetic Protein Chemistry/Chemical Biology/Biochemistry

Chemical approaches to study protein modifications The complexity of cellular processes in higher organisms is in stark contrast with the relatively few protein-coding genes (~21,000) in their cells. The chemical modification of proteins after they are assembled on ribosomes, termed protein post-translational modification (PTM), is an important process that adds rich diversity to protein function. We are broadly interested in understanding how chemical modifications affect protein structure and function. Our specific focus is on studying protein modification by small ubiquitin-like proteins. We combine the powerful tools of synthetic organic chemistry and molecular biology to generate specifically modified proteins that are subjected to biochemical and biophysical investigation. Students in our group gain expertise in the synthesis, purification, and characterization of small molecules and proteins. Two current areas of research are histone protein modification by the small ubiquitin-like protein modifier, SUMO, and modification of Mycobacterium tuberculosis proteins by the prokaryotic ubiquitin-like protein, Pup. We believe that understanding how these proteins modify the functions of their targets will allow us to devise new ways to control gene function and bacterial infection.

近期论文

查看导师新发文章 （温馨提示：请注意重名现象，建议点开原文通过作者单位确认）

Miller, L.M.; Menthena, A.: Chatterjee, C.; Verdier-Pinard, P.; Novikoff, P. Horwitz, S.B.; Angeletti, R.H. "Increased levels of a unique post-translationally modified bIVb-tubulin isotype in liver cancer." Biochemistry 2008, 47, 7572-7582. McGinty, R.K.; Kim, J.; Chatterjee, C.; Roeder, R.G.; Muir, T.W. "Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation." Nature 2008, 453, 812-816. Chatterjee, C.; McGinty, R.K.; Pellois, J.-P.; Muir, T.W. "Auxiliary-mediated site-specific peptide ubiquitylation." Angew. Chem. Int. Ed. Engl. 2007, 46, 2814-2818. Chatterjee, C.*; Patton, G.C.*; Cooper, L.; Paul, M.; van der Donk, W.A. Engineering dehydro amino acids and thioethers into peptides using Lacticin 481 synthetase Chemistry and Biology 2006, 13, 1109-1117. Miller, L.M.; Chatterjee, C.; van der Donk, W.A.; Kelleher, N.L. The dehydratase activity of Lacticin 481 synthetase is highly processive J. Am. Chem. Soc. 2006, 128, 1420-121. Chatterjee, C.; Miller, L.M.; Leung, Y.L.; Xie, L.; Yi, M.; Kelleher, N.L.; van der Donk, W.A. Lacticin 481 synthetase phosphorylates its substrate during lantibiotic production J. Am. Chem. Soc. 2005, 127, 15332-15333. Xie, L.; Miller, L.M.; Chatterjee, C.; Averin, O.; Kelleher, N.L.; van der Donk, W.A. Lacticin 481: in vitro reconstitution of lantibiotic synthetase activity Science 2004, 303, 679-681. Xie, L.; Chatterjee, C.; Balsara, R.; Okeley, N.M.; van der Donk, W.A. Heterologous expression and purification of SpaB involved in subtilin biosynthesis Biochem. Biophys. Res. Commun. 2002, 295, 952-957. Chatterjee, C.; Paul, M.; Xie, L.; van der Donk, W.A. Biosynthesis and mode of action of lantibiotics Chem. Rev. 2005, 105, 633-683. McGinty, R.K.; Chatterjee, C.; Muir, T.W. Semisynthesis of ubiquitylated proteins Methods Enzymol. 2009, 462, 225-243. Chatterjee, C.; Muir, T. W. Chemical approaches for studying histone modifications J. Biol. Chem. 2010, doi:10.1074/jbc.R109.080291 Fierz, B.; Chatterjee, C.; McGinty, R.K.; Muir, T.W. Ubiquitylated H2B acts as a molecular wedge disrupting chromatin fibres (under revision at Nature)