PXD021948

PXD021948 is an original dataset announced via ProteomeXchange.

Title	Chemical Tagging of Protein Lipoylation
Description	Protein lipoylation is a post-translational modification of emerging importance in both prokaryotes and eukaryotes. However, effective methods for labeling and analyzing, particularly in large scale, protein lipoylation remain limited. Here, we report the development of iLCL (iodoacetamide-assisted lipoate-cyclooctyne ligation), a chemoselective reaction that enables chemical tagging of protein lipoylation. We demonstrate that the cyclic disulfide of lipoamide but not linear disulfides can selectively react with iodoacetamide to produce sulfenic acid, which can be conjugated with cyclooctyne probes. Using iLCL, lipoylation on recombinant bacterial lipoylated proteins and in cell and tissue lysates is tagged with fluorophores for analysis by in-gel fluorescence scanning and cellular imaging. Furthermore, we apply iLCL for proteomic profiling of lipoylated proteins in both bacteria and mammalian cells. In addition to all of the eight known lipoylated proteins, seven new ones are identified. The iLCL-based tagging method should facilitate the studies and understanding of biological function of protein lipoylation.
HostingRepository	PRIDE
AnnounceDate	2020-11-16
AnnouncementXML	Submission_2020-11-16_07:46:41.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Qi Tang
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562; scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationList	iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2020-10-13 03:23:05	ID requested
⏵ 1	2020-11-16 07:46:41	announced

Dataset with its publication pending

submitter keyword: lipoylation, chemical proteomics, chemoselective ligation

Xing Chen
contact affiliation	College of Chemistry and Molecular Engineering, Peking University, Beijing, China.
contact email	xingchen@pku.edu.cn
lab head
Qi Tang
contact affiliation	College of Chemistry and Molecular Engineering, Peking University
contact email	tangqi@pku.edu.cn
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD021948
     1. Label: PRIDE project
     2. Name: Chemical Tagging of Protein Lipoylation