PXD004053

PXD004053 is an original dataset announced via ProteomeXchange.

Title	Global profiling and inhibition of protein lipidation in vector and host stages of the sleeping sickness parasite Trypanosoma brucei via chemical proteomics
Description	The enzyme N-myristoyltransferase (NMT) catalyses the essential fatty acylation of substrate proteins with myristic acid in eukaryotes and is a validated drug target in the parasite Trypanosoma brucei, the causative agent of African trypanosomiasis (sleeping sickness). N-Myristoylation typically mediates membrane localisation of proteins and is essential to the function of many. However, only a handful of proteins are experimentally validated as N-myristoylated in T. brucei. Here, we perform metabolic labelling with an alkyne-tagged myristic acid analogue (“YnMyr”), enabling the capture of lipidated proteins in insect (PCF) and host (BSF) life stages of T. brucei. We further compare this with a longer chain palmitate analogue (“YnPal”) to explore the chain length-specific incorporation of fatty acids into proteins. Finally, we combine the alkynyl-myristate analogue with NMT inhibitors (Cpds 1 and 2) and quantitative chemical proteomics to globally define N-myristoylated proteins in the clinically relevant bloodstream form parasites.
HostingRepository	PRIDE
AnnounceDate	2016-05-17
AnnouncementXML	Submission_2016-05-17_11:09:04.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Megan Wright
SpeciesList	scientific name: Trypanosoma brucei; NCBI TaxID: 5691;
ModificationList	iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2016-04-26 02:37:51	ID requested
⏵ 1	2016-05-17 11:09:05	announced

Dataset with its publication pending

curator keyword: Biomedical

submitter keyword: Human African trypanosomiasis, N-myristoylation, chemical proteomics, click chemistry, protein lipidation, target validation

Edward William Tate
contact affiliation	Department of Chemistry, Imperial College London
contact email	e.tate@imperial.ac.uk
lab head
Megan Wright
contact affiliation	Technical University of Munich
contact email	megan.wright@tum.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD004053
     1. Label: PRIDE project
     2. Name: Global profiling and inhibition of protein lipidation in vector and host stages of the sleeping sickness parasite Trypanosoma brucei via chemical proteomics