PXD004326

PXD004326 is an original dataset announced via ProteomeXchange.

Title	Metabolic regulation of N-terminal acetylation in yeast
Description	N-terminal (Nt) acetylation, catalyzed by N-terminal acetyltransferases (NATs), has emerged as an important co-translational modification in eukaryotes, and involves the transfer of the acetyl moiety from acetyl-CoA (Ac-CoA) to the α-amino group of a nascent polypeptide. Here, we report the first global study of Nt-acetylation in response to changes in nutrient availability in S. cerevisiae. Despite major fluctuations in Ac-CoA and histone acetylation levels, our study reveals that the steady-state levels of protein Nt-acetylation remains largely unaffected by changes in cellular metabolism. Accordingly, Ac-CoA does not appear to act as a master switch for protein Nt-acetylation. Interestingly however, we identified two distinct sets of N-termini that are differentially Nt-acetylated following nutrient starvation. The first set of proteins, enriched for annotated N-termini, generally displayed an increased Nt-acetylation in stationary phase compared to exponential growth phase, despite a significant reduction in Ac-CoA levels. In contrast, the second set of proteins, enriched for alternative non-annotated N-termini (i.e. N-terminal proteoforms), generally became less acetylated in stationary phase. In particular, the degree of Nt-acetylation of Pcl8, a negative regulator of glycogen biosynthesis and two components of the pre-ribosome complex (Rsa3 and Rpl7a) increased during starvation. Moreover, the levels of these proteins were regulated by both starvation and the presence of NatA activity. Overall, our data provide the first proteome-wide survey on metabolic regulation of Nt-acetylation, and propose Nt-acetylation-mediated steering of metabolism and ribosome biogenesis.
HostingRepository	PRIDE
AnnounceDate	2018-09-07
AnnouncementXML	Submission_2018-09-07_04:12:57.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Petra Van Damme
SpeciesList	scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationList	acetylated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap

Revision	Datetime	Status	ChangeLog Entry
0	2016-06-14 08:50:03	ID requested
⏵ 1	2018-09-07 04:12:58	announced

Varland S, Aksnes H, Kryuchkov F, Impens F, Van Haver D, Jonckheere V, Ziegler M, Gevaert K, Van Damme P, Arnesen T, . Mol Cell Proteomics, 17(12):2309-2323(2018) [pubmed]

curator keyword: Biological

submitter keyword: N-terminal Acetylation, Acetyl coenzyme A, Metabolism, Saccharomyces cerevisiae, N-terminomics

Petra Van Damme
contact affiliation	Medical Biotechnology Center, VIB, B-9000 Ghent, Belgium, Department of Biochemistry, Ghent University, B-9000 Ghent, Belgium.
contact email	Petra.vandamme@vib-ugent.be
lab head
Petra Van Damme
contact affiliation	University of Ghent
contact email	petra.vandamme@ugent.be
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/2018/09/PXD004326

PRIDE project URI

• PRIDE
  1. PXD004326
     1. Label: PRIDE project
     2. Name: Metabolic regulation of N-terminal acetylation in yeast