PXD020740-1

PXD020740 is an original dataset announced via ProteomeXchange.

Title	Chemical proteomics profiling of the alarmones diadenosine triphosphate and tetraphosphate reveals their comprehensive protein interaction networks
Description	Abstract Diadenosine triphosphate (Ap3A) and diadenosine tetraphosphate (Ap4A) are formed in prokaryotic and eukaryotic cells. Since their concentrations increase significantly upon cellular stress they were considered to be alarmones triggering stress adaptive processes. However, their exact role remains elusive. To elucidate the proteome-wide interactome of Ap3A and Ap4A and gain insights into their intracellular roles, we herein report the development of new photoaffinity-labeling probes and their employment in chemical proteomics using eukaryotic and prokaryotic cells. We found the involvement of the ApnA interactors in many fundamental cellular process including carboxylic acid and nucleotide metabolism, gene expression, various regulatory processes and stress response. Our results highlight common roles of these ApnAs across the domains of life, but also roles that are different for Ap3A or Ap4A. This study provides a rich source for further functional studies of these nucleotides and depicts useful tools for characterisation of their regulatory mechanisms in cells.
HostingRepository	PRIDE
AnnounceDate	2022-02-16
AnnouncementXML	Submission_2022-02-16_04:12:29.042.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Lena Krüger
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562; scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2020-08-05 09:39:58	ID requested
⏵ 1	2022-02-16 04:12:30	announced
2	2022-03-09 04:38:27	announced	2022-03-09: Updated project metadata.

Kr, ü, ger L, Albrecht CJ, Schammann HK, Stumpf FM, Niedermeier ML, Yuan Y, Stuber K, Wimmer J, Stengel F, Scheffner M, Marx A, Chemical proteomic profiling reveals protein interactors of the alarmones diadenosine triphosphate and tetraphosphate. Nat Commun, 12(1):5808(2021) [pubmed]

submitter keyword: diadenosine polyphosphates, photo-affinity labeling, interction studies

Andreas Marx
contact affiliation	1Department of Chemistry, University of Konstanz, Konstanz, Germany 2Konstanz Resea1Department of Chemistry, University of Konstanz, Konstanz, Germany 2Konstanz Research School-Chemical Biology, University of Konstanz, Konstanz, Germany
contact email	andreas.marx@uni-konstanz.de
lab head
Lena Krüger
contact affiliation	University of Konstanz
contact email	lena.krueger@uni-konstanz.de
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/2022/02/PXD020740

PRIDE project URI

• PRIDE
  1. PXD020740
     1. Label: PRIDE project
     2. Name: Chemical proteomics profiling of the alarmones diadenosine triphosphate and tetraphosphate reveals their comprehensive protein interaction networks