BEGIN:VCALENDAR
VERSION:2.0
PRODID:-//Memento EPFL//
BEGIN:VEVENT
SUMMARY:Studying ubiquitin-like proteins across the domains of life
DTSTART:20191203T161500
DTEND:20191203T173000
DTSTAMP:20260506T220949Z
UID:71c16c7a57bb7b30c5014fd8a53227b8b1af686ce5b8e451ae5800b7
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Champak Chatterjee\, Department of Chemistry\, Universi
 ty of Washington (USA) \nThe group of Champak Chatterjee has developed ch
 emical probes and synthetic strategies to study two ubiquitin family prote
 ins – the prokaryotic ubiquitin-like protein (Pup) in Mycobacterium tube
 rculosis\, and the small ubiquitin-like modifier protein (SUMO) in humans.
  Chatterjee will present key insights on the mechanism of protein pupylati
 on\, that led him to the development of peptide inhibitors. He will also d
 escribe biochemical studies with chemically sumoylated histones and propos
 e a model for gene regulation by SUMO.\n\nTalk abstract\nThe prokaryotic u
 biquitin-like protein (Pup) is found in the disease-causing bacterium Myc
 obacterium tuberculosis that infects about a third of the world’s popul
 ation. Protein modification by Pup\, called pupylation\, is necessary for 
 the persistence of tuberculosis infection. Hence\, the enzymes associated 
 with pupylation are potentially new targets in drug-resistant tuberculosis
 . Chatterjee lab has developed new chemical probes for mechanistic studies
  of the enzymes associated with protein pupylation. Key insights gained fr
 om biochemical studies with these probes\, which led to the development of
  peptide inhibitors of protein pupylation will be presented.\nIn contrast 
 with Pup\, the small ubiquitin-like modifier protein\, SUMO\, is a human p
 rotein critical for gene regulation and repair. Lysine side-chain modifica
 tion by SUMO is a conserved modification of many important nuclear protein
 s\, such as transcription factors and histones. Chatterjee lab has develop
 ed facile chemical strategies to synthesize human proteins modified by SUM
 O. Champak Chatterjee will present results from biophysical and biochemica
 l studies enabled by his synthesis\, and propose a model for gene regulati
 on by histone sumoylation.\n \nAbout Champak Chatterjee\nChampak received
  his B.Sc. in Chemistry (First Class) from the University of Bombay\, and 
 an M.Sc. in Organic Chemistry from I.I.T. Bombay (Institute Silver Medal)\
 , where he synthesized non-natural amino acids in the laboratory of Prof. 
 Sambasivarao Kotha. Champak then moved to the U.S. and performed doctoral 
 studies in the research group of Prof. Wilfred van der Donk at the Univers
 ity of Illinois at Urbana-Champaign. At Illinois\, Champak studied the mec
 hanism of biosynthesis of a class of ribosomally synthesized and post-tran
 slationally modified peptide antibiotics called lantibiotics or RiPPs. His
  post-doctoral work in Prof. Tom Muir’s laboratory at the Rockefeller Un
 iversity focused on understanding the mechanism by which ubiquitin stimula
 tes histone methylation\, and developing new methods for the site-specific
  modification of proteins.\nChampak Chatterjee webpage\n \nMajor publicat
 ions\n\n	Smirnov\, D.\; Dhall\, A.\; Sivanesam\, K.\; Sharar\, R. J.\; Cha
 tterjee\, C.\, “Fluorescent probes reveal a minimal ligase recognition m
 otif in the prokaryotic ubiquitin-like protein from Mycobacterium tubercu
 losis”\, Am. Chem. Soc.2013.\n	Weller\, C.E.\; Dhall\, A.\; Ding\, F.\;
  Linares\, E.\; Whedon\, S.D.\; Senger\, N.A.\; Tyson\, E.L.\; Bagert\, J.
 D.\; Li\, X.\; Augusto\, O.\; Chatterjee\, C.\, “Aromatic thiol-mediated
  cleavage of N-O bonds enables chemical ubiquitylation of folded proteins
 ”\, Nature Communications.\n	Dhall\, A.\; Weller\, C.E.\; Chu\, A.\; Sh
 elton\, P.M.M.\; Chatterjee\, C.\, “Chemically sumoylated histone H4 sti
 mulates intranucleosomal demethylation by the LSD1-CoREST complex”\, AC
 S Chemical Biology.\n	Stewart\, M.D.\; Zelin\, E.\; Dhall\, A.\; Walsh\, T
 .\; Upadhyay\, E.\; Corn\, J.E.\; Chatterjee\, C.\; King\, M.-C.\; Klevit\
 , R.E.\, “BARD1 is necessary for ubiquitylation of nucleosomal histone H
 2A and for transcriptional regulation of estrogen metabolism genes”\, N
 atl. Acad. Sci. U.S.A. 2018.\n	Hsu\, L.P.\; Shi\, H.\; Leonen\, C.L.\; Ka
 ng\, J.\; Chatterjee\, C.*\; Zheng\, N.*\, “Structural basis of H2B ubiq
 uitination-dependent H3K4 methylation by COMPASS”\, Molecular Cell (*c
 o-corresponding)\n
LOCATION:BCH 2201 https://plan.epfl.ch/theme/generalite_thm_v2?request_loc
 ale=en&room=BCH%202201&domain=places&dim_floor=2&lang=en&dim_lang=en&tree_
 groups=centres_nevralgiques%2Cacces%2Cmobilite_reduite%2Censeignement&
STATUS:CONFIRMED
END:VEVENT
END:VCALENDAR