PXD000924

PXD000924 is an original dataset announced via ProteomeXchange.

Title	Vibrio parahaemolyticus LC-MS/MS
Description	The lysine acetylation of proteins is a major post-translational modification that plays an important regulatory role in almost every aspect of cells, both eukaryotes and prokaryotes. Vibrio parahaemolyticus, a model marine bacterium, is a worldwide cause of bacterial seafood-borne illness. Here, we conducted the first lysine acetylome in the bacterium through combination of highly sensitive immune-affinity purification and high-resolution LC-MS/MS. Overall, we identified 1413 lysine acetylation sites in 656 proteins, which account for 13.6% of the total proteins in the cells and is the highest ratio of acetyl proteins that has so far been identified in bacteria. The bioinformatics analysis of the acetylome showed that the acetylated proteins are involved in a wide range of cellular functions and exhibit diverse subcellular localizations. More specifically, proteins related to protein biosynthesis and carbon metabolism are the preferential targets of lysine acetylation. Moreover, two types of acetylation motifs, a lysine or arginine at the +4/+5 position and a tyrosine, histidine, or phenylalanine at the +1/+2 position, were revealed from the analysis of the acetylome. Additionally, the protein interaction network analysis demonstrates that a wide range of interactions are modulated by protein acetylation. This study provides a significant beginning for the in-depth exploration of the physiological role of lysine acetylation in V. parahaemolyticus.
HostingRepository	PRIDE
AnnounceDate	2017-08-23
AnnouncementXML	Submission_2017-08-23_04:20:07.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD000924
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Jianyi Pan
SpeciesList	scientific name: Vibrio paraaemolytics RIMD 2210633; NCBI TaxID: 223926;
ModificationList	monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2014-04-23 08:02:37	ID requested
⏵ 1	2017-08-23 04:20:09	announced

Pan J, Ye Z, Cheng Z, Peng X, Wen L, Zhao F, Systematic analysis of the lysine acetylome in Vibrio parahemolyticus. J Proteome Res, 13(7):3294-302(2014) [pubmed]

curator keyword: Biological, Biomedical

submitter keyword: lysine acetylation, acetylome, lysine acetylation motif, interaction network, V. parahaemolyticus

Jianyi Pan
contact affiliation	Institute of Proteomics and Molecular Enzymology, School of Life Sciences, Zhejiang Sci-Tech University
contact email	panjy@zstu.edu.cn
lab head
Jianyi Pan
contact affiliation	Zhejiang Sci-Tech University
contact email	panjy@zstu.edu.cn
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD000924
     1. Label: PRIDE project
     2. Name: Vibrio parahaemolyticus LC-MS/MS