PXD045925

PXD045925 is an original dataset announced via ProteomeXchange.

Title	Pronucleotide probes reveal a diverging specificity for AMPylation vs. UMPylation of human and bacterial nucleotide transferases
Description	AMPylation is a post-translational modification utilized by human and bacterial cells to modulate the activity and function of specific proteins. Major AMPylators such as human FICD and bacterial VopS have been studied extensively for their substrate and target scope in vitro. Recently, an AMP pronucleotide probe also facilitated the in situ analysis of AMPylation in living cells. Based on this technology we here introduce a novel UMP pronucleotide probe and utilize it in the profiling of uninfected and Vibrio parahaemolyticus infected human cells. Mass spectrometric analysis of labeled protein targets reveals an unexpected promiscuity of human nucleotide transferases with an almost identical target set of AMP- and UMPylated proteins. Vice versa, studies in cells infected by V. parahaemolyticus and its effector VopS revealed solely AMPylation of host enzymes highlighting a so far unknown specificity of this transferase for ATP. Taken together, pronucleotide probes provide an unprecedented insight into the in situ activity profile of crucial nucleotide transferases which can largely differ compared to their in vitro activity.
HostingRepository	PRIDE
AnnounceDate	2024-02-27
AnnouncementXML	Submission_2024-02-27_02:45:39.993.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Dietrich Mostert
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2023-10-06 01:37:27	ID requested
⏵ 1	2024-02-27 02:45:40	announced

Mostert D, Bubeneck WA, Rauh T, Kielkowski P, Itzen A, Jung K, Sieber SA, Pronucleotide Probes Reveal a Diverging Specificity for AMPylation vs UMPylation of Human and Bacterial Nucleotide Transferases. Biochemistry, 63(5):651-659(2024) [pubmed]

10.1021/acs.biochem.3c00568;

submitter keyword: Infection, AMPylation, VopS,UMPylation, Pronucleotide

Stephan A. Sieber
contact affiliation	Center for Functional Protein Assemblies (CPA), Department of Chemistry, Chair of Organic Chemistry II, Technical University of Munich, 85748 Garching, Germany
contact email	stephan.sieber@tum.de
lab head
Dietrich Mostert
contact affiliation	Center for Functional Protein Assemblies (CPA), Department of Chemistry, Chair of Organic Chemistry II, Technical University of Munich, 85748 Garching, Germany.
contact email	dietrich.mostert@tum.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/2024/02/PXD045925

PRIDE project URI

• PRIDE
  1. PXD045925
     1. Label: PRIDE project
     2. Name: Pronucleotide probes reveal a diverging specificity for AMPylation vs. UMPylation of human and bacterial nucleotide transferases