PXD006272

PXD006272 is an original dataset announced via ProteomeXchange.

Title	Systematic analysis of the lysine acetylome reveals diverse functions of lysine acetylation in the oleaginous yeast Yarrowia lipolytica
Description	Lysine acetylation of proteins, a major post-translational modification, plays a critical regulatory role in almost every aspects in both eukaryotes and prokaryotes. Yarrowia lipolytica, an oleaginous yeast, is considered as a model for bio-oil production due to its ability to accumulate a large amount of lipids. However, the function of lysine acetylation in this organism is elusive. Here, we performed a global acetylproteome analysis of Y. lipolytica ACA-DC 50109. In total, 3163 lysine acetylation sites were identified in 1428 proteins, which account for 22.1% of the total proteins in the cell. Fifteen conserved acetylation motifs were detected. The acetylated proteins participate in a wide variety of biological processes. Notably, a total of 65 enzymes involved in lipid biosynthesis were found to be acetylated. The acetylation sites are distributed in almost every type of conserved domains in the multi-enzymatic complexes of fatty acid synthetases, suggesting an important regulatory role of lysine acetylation in lipid metabolism. Moreover, protein interaction network analysis reveals that diverse interactions are modulated by protein acetylation. The provided dataset probably illuminates the crucial role of reversible acetylation in oleaginous microorganisms, and serves as an important resource for exploring the physiological role of lysine acetylation in eukaryotes.
HostingRepository	PRIDE
AnnounceDate	2018-11-22
AnnouncementXML	Submission_2018-11-22_02:45:12.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Lin Liu
SpeciesList	scientific name: Yarrowia lipolytica (Candida lipolytica); NCBI TaxID: 4952;
ModificationList	acetylated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2017-04-10 01:25:57	ID requested
⏵ 1	2018-11-22 02:45:13	announced

Wang G, Guo L, Liang W, Chi Z, Liu L, Systematic analysis of the lysine acetylome reveals diverse functions of lysine acetylation in the oleaginous yeast Yarrowia lipolytica. AMB Express, 7(1):94(2017) [pubmed]

curator keyword: Biological

submitter keyword: Lysine acetylation, Acetylproteome, Yarrowia lipolytica, Oleaginous yeast, Lipid biosynthesis

Wenxing Liang
contact affiliation	2The Key Laboratory of Integrated Crop Pest Management of Shandong Province, College of Agronomy and Plant Protection, Qingdao Agricultural University, Qingdao 266109, China
contact email	wliang1@qau.edu.cn
lab head
Lin Liu
contact affiliation	College of Life Sciences, Qingdao Agricultural University, Qingdao 266109, China
contact email	liulin@qau.edu.cn
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD006272
     1. Label: PRIDE project
     2. Name: Systematic analysis of the lysine acetylome reveals diverse functions of lysine acetylation in the oleaginous yeast Yarrowia lipolytica