PXD031466

PXD031466 is an original dataset announced via ProteomeXchange.

Title	Quantitative Site-specific Chemoproteomic Profiling of Protein Lipoylation
Description	Protein lipoylation is an evolutionarily conserved post-translational modification (PTM) from prokaryotes and eukary-otes. Lipoylation is known to contribute to several human diseases including metabolic disorders, cancer and Alz-heimer’s disease. While individual lipoylated proteins have been biochemically studied, a strategy for globally quantify-ing lipoylation sites in proteomes is lacking. Herein we developed a butyraldehyde-alkynyl probe (BAP) to specifically label and enrich lipoylations in complexed biological samples. Combined with a chemoproteomic pipeline with cus-tomized tandem enzyme digestion protocols and a biotin enrichment tag with enhanced ionization, we successfully quantified all known lipoylation sites in both E. coli and human proteomes. The strategy enabled us to dissect the de-pendence of the three evolutionarily related lipoylation sites in dihydrolipoamide acetyltransferase (ODP2) in Esche-richia coli and evaluated the functional connection between the de novo lipoylation synthetic pathway and the salvage pathway. The study also led to the discovery that lipoate-protein ligase A (LplA) could replace octanoic acid transferase (LipB) to perform the function of transferring octanoic acid in the de novo synthetic pathway when octanoic acids are abundant. Our chemoproteomic platform provides a useful tool to monitor the state of lipoylation in proteome samples, which might help decipher molecular mechanisms of lipoylation-related diseases.
HostingRepository	iProX
AnnounceDate	2022-02-05
AnnouncementXML	Submission_2023-12-24_20:36:58.839.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Shuchang Lai
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562; scientific name: Homo sapiens; NCBI TaxID: 9606;
ModificationList	N6-lipoyl-L-lysine
Instrument	Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2022-02-05 21:46:34	ID requested
1	2022-02-05 21:46:58	announced
⏵ 2	2023-12-24 20:36:59	announced	2023-12-25: Update information.

Lai S, Chen Y, Yang F, Xiao W, Liu Y, Wang C, Quantitative Site-Specific Chemoproteomic Profiling of Protein Lipoylation. J Am Chem Soc, 144(23):10320-10329(2022) [pubmed]

submitter keyword: Lipoylation, butyraldehyde probe (BAP), Quantitative chemoproteomics.

Chu Wang
contact affiliation	Peking University
contact email	chuwang@pku.edu.cn
lab head
Shuchang Lai
contact affiliation	Peking University
contact email	shuchanglai@pku.edu.cn
dataset submitter

iProX dataset URI