PXD012023

PXD012023 is an original dataset announced via ProteomeXchange.

Title	Serine-Threonine Kinase Encoded by a Split hipA Homologous Gene of Escherichia coli Inhibits Tryptophanyl-tRNA Synthetase
Description	Type II toxin – antitoxin modules encode a stable toxin that inhibits translation, replication or cell wall synthesis and an unstable protein antitoxin that neutralizes the toxin by direct protein – protein contact. The hipBA module of Escherichia coli K-12 codes for HipA, a eukaryote-like serine/threonine protein kinase that phosphorylates and inhibits glutamyl-tRNA synthetase. Induction of hipA leads to a reduced level of charged glutamyl tRNA that, in turn, inhibits translation, induces RelA-dependent (p)ppGpp synthesis and multidrug tolerance (persistence). Here, we describe the discovery of a three-component TA module hipBST of E. coli O127:H6 strain E2348/69 that encodes HipT, which exhibits sequence similarity with the C-terminal part of HipA. We show that HipT is a kinase that phosphorylates tryptophanyl-tRNA synthetase in vitro at conserved serine residue. Consistently, induction of hipT inhibits cell growth, stimulates production of stringent factor (p)ppGpp and induces persistence. Remarkably, the gene immediately upstream of hipT, called hipS, encodes a small protein that exhibits sequence similarity with the C-terminal part of HipA. Unexpectedly, HipT kinase is neutralized by HipS in vivo whereas the third component, HipB0127, encoded by the first gene of the operon, does not counteract HipT kinase. However, HipB contains a HTH DNA-binding domain and may function to autoregulate the hipBST operon. Thus, hipA has been split into two genes, hipS and hipT that function as a toxin – antitoxin pair.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_03:58:24.764.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Nicolas Nalpas
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	phosphorylated residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2018-12-12 00:01:32	ID requested
1	2019-06-24 07:41:16	announced
2	2019-06-28 03:29:38	announced	Updated publication reference for PubMed record(s): 31213559.
⏵ 3	2024-10-22 03:58:25	announced	2024-10-22: Updated project metadata.

10.1128/mBio.01138-19;

Vang Nielsen S, Turnbull KJ, Roghanian M, B, æ, rentsen R, Semanjski M, Brodersen DE, Macek B, Gerdes K, Homologs Inhibit Tryptophanyl-tRNA Synthetase. mBio, 10(3):(2019) [pubmed]

curator keyword: Biological

submitter keyword: E. coli, kinase,phosphorylation

Boris Macek
contact affiliation	Quantitative Proteomics & Proteome Center Tuebingen Interfaculty Institute for Cell Biology University of Tuebingen Tuebingen Germany
contact email	boris.macek@uni-tuebingen.de
lab head
Nicolas Nalpas
contact affiliation	University of Rouen
contact email	nalpas.nicolas@gmail.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/2019/06/PXD012023

PRIDE project URI

• PRIDE
  1. PXD012023
     1. Label: PRIDE project
     2. Name: Serine-Threonine Kinase Encoded by a Split hipA Homologous Gene of Escherichia coli Inhibits Tryptophanyl-tRNA Synthetase