CHEMPROT-HLMS

Chemical proteomics for universal profiling of histone lysine malonylation and succinylation

Coordinatore	IMPERIAL COLLEGE OF SCIENCE, TECHNOLOGY AND MEDICINE    more  Organization address address: SOUTH KENSINGTON CAMPUS EXHIBITION ROAD city: LONDON postcode: SW7 2AZ contact info Titolo: Ms. Nome: Brooke Cognome: Alasya Email: send email Telefono: +44 207 594 1181 Fax: +44 207 594 1418
Nazionalità Coordinatore	United Kingdom [UK]
Totale costo	221˙606 €
EC contributo	221˙606 €
Programma	FP7-PEOPLE Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
Code Call	FP7-PEOPLE-2012-IEF
Funding Scheme	MC-IEF
Anno di inizio	2013
Periodo (anno-mese-giorno)	2013-07-01   -   2015-06-30

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	IMPERIAL COLLEGE OF SCIENCE, TECHNOLOGY AND MEDICINE  Organization address address: SOUTH KENSINGTON CAMPUS EXHIBITION ROAD city: LONDON postcode: SW7 2AZ contact info Titolo: Ms. Nome: Brooke Cognome: Alasya Email: send email Telefono: +44 207 594 1181 Fax: +44 207 594 1418	UK (LONDON)	coordinator	221˙606.40

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 Obiettivo del progetto (Objective)

A large body of evidence suggest that reversible post-translational modifications (PTMs) of histones play a crucial role in gene expression and to the field of epigenetics, and that aberrant histone modification contributes to different diseases such as cancer. Recently, two novel types of histone PTMs called lysine malonylation (Kmal) and succinylation (Ksucc) have been identified. KMal and Ksucc induce more substantial chemical changes to the chemical properties of the modified protein than lysine acetylation or methylation, which are already known to have very important cellular roles. Taking into account the fact that most previously described histone PTMs have important biological functions and are implied in different human diseases, a logical hypothesis is that Ksucc and Kmal also play an important role in the regulation of histone protein structure and function, and potentially also across the wider proteome. These novel PTMs open many interesting questions: • Which histone lysine residues are the targets for these novel PTMs? • What enzymes regulate addition (writer) or removal (eraser) of Kmal and Ksucc? • Are there reader proteins that bind to histone Kmal and Ksucc to modulate changes in gene transcription? • What role do histone Kmal and Ksucc play in the regulation of histone structure and function? However, there are no standard and robust tools to directly identify and manipulate the enzymes or binders, and identifying the targets is currently a massive undertaking, and it is not easy to ‘pulse-chase’ without a label. The aim of the proposed project is to develop a platform of chemical probes and technologies that will enable for the first time proteome-wide global analysis of the complex biological network involve in these new types of PTMs of histone. These novel chemical biology tools will be used to identify novel histone targets and the enzymes (writers and erasers) and proteins (readers) involved in these new PTMs.