PXD004802

PXD004802 is an original dataset announced via ProteomeXchange.

Title	Proteome-wide profiling of protein lysine acetylation in Aspergillus flavus
Description	Protein lysine acetylation is a prevalent post-translational modification that plays pivotal roles in various biological processes in both prokaryotes and eukaryotes. Aspergillus flavus, as a fungus of aflatoxin producer, has attracted tremendous attention due to its health impact on agricultural commodities. Here, we performed the first lysine-acetylome mapping in this filamentous fungus using immune-affinity-based purification integrated with high-resolution mass spectrometry. Overall, we identified 1383 lysine-acetylation sites in 652 acetylated proteins, which account for 5.18% of the total proteins in A. flavus. The acetylated proteins are involved in various cellular processes involving the ribosome, carbon metabolism, antibiotic biosynthesis, secondary metabolites, and the citrate cycle and are distributed in diverse subcellular locations according to bioinformatics analysis. We demonstrated for the first time the acetylation of fatty acid synthase α and β encoded by aflA and aflB involved in the aflatoxin-biosynthesis pathway (cluster 54), as well as backbone enzymes from secondary metabolite clusters 20 and 21 encoded by AFLA_062860 and AFLA_064240, suggesting important roles for acetylation associated with these processes. Our findings illustrating abundant lysine acetylation in A. flavus expanded the understanding of the fungal acetylome and provided insight into the regulatory roles of acetylation in secondary metabolism.
HostingRepository	PRIDE
AnnounceDate	2017-06-12
AnnouncementXML	Submission_2017-06-12_04:22:21.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Yuansen Hu
SpeciesList	scientific name: Aspergillus flavus; NCBI TaxID: 5059;
ModificationList	acetylated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2016-08-15 03:01:00	ID requested
⏵ 1	2017-06-12 04:22:22	announced

Lv Y, Proteome-wide profiling of protein lysine acetylation in Aspergillus flavus. PLoS One, 12(6):e0178603(2017) [pubmed]

curator keyword: Biological

submitter keyword: acetylation aspergillus flavus

Yangyong Lv
contact affiliation	College of Biological Engineering, Henan University of Technology, Zhengzhou, China
contact email	lvyangyong2011@163.com
lab head
Yuansen Hu
contact affiliation	College of Biological Engineering, Henan University of Technology, Zhengzhou, China
contact email	hys308@126.com
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2017/06/PXD004802

PRIDE project URI

• PRIDE
  1. PXD004802
     1. Label: PRIDE project
     2. Name: Proteome-wide profiling of protein lysine acetylation in Aspergillus flavus