PXD005236

PXD005236 is an original dataset announced via ProteomeXchange.

Title	A bacteriophage enzyme induces bacterial metabolic perturbation that confers a novel promiscuous function
Description	One key concept in the evolution of new functions is the ability of enzymes to perform promiscuous side-reactions that serve as a source of novelty that may become beneficial under certain conditions. Here, we identify a mechanism where a bacteriophage-encoded enzyme introduces novelty by inducing expression of a promiscuous bacterial enzyme. By screening for bacteriophage DNA that rescued an auxotrophic E. coli mutant carrying a deletion of the ilvA gene, we show that bacteriophage-encoded S-adenosylmethionine (SAM) hydrolases reduce SAM levels. Via this perturbation of bacterial metabolism, expression of the promiscuous bacterial enzyme MetB is increased, which in turn complements the absence of IlvA. These results demonstrate how foreign DNA can increase the metabolic capacity of bacteria, not only by transfer of bona fide new genes, but also by bringing cryptic bacterial functions to light via perturbations of cellular physiology.
HostingRepository	PRIDE
AnnounceDate	2018-05-11
AnnouncementXML	Submission_2018-06-05_04:51:01.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Egor Vorontsov
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	TMT6plex-126 reporter+balance reagent acylated residue; monohydroxylated residue
Instrument	Orbitrap Fusion ETD

Revision	Datetime	Status	ChangeLog Entry
0	2016-10-28 02:24:38	ID requested
1	2018-05-11 04:03:16	announced
⏵ 2	2018-06-05 04:51:02	announced	Updated publication reference for PubMed record(s): 29807996.

Jerlstr, ö, m Hultqvist J, Warsi O, S, ö, derholm A, Knopp M, Eckhard U, Vorontsov E, Selmer M, Andersson DI, A bacteriophage enzyme induces bacterial metabolic perturbation that confers a novel promiscuous function. Nat Ecol Evol, 2(8):1321-1330(2018) [pubmed]

curator keyword: Biological

submitter keyword: Escherichia coli, antibiotic resistance, TMT, Orbitrap Fusion

Dan I. Andersson
contact affiliation	Department of Medical Biochemistry and Microbiology, Uppsala University, Box 582, 75123, Uppsala, Sweden
contact email	Dan.Andersson@imbim.uu.se
lab head
Egor Vorontsov
contact affiliation	Proteomics Core Facility, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden
contact email	yegor.msu@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/2018/05/PXD005236

PRIDE project URI

• PRIDE
  1. PXD005236
     1. Label: PRIDE project
     2. Name: A bacteriophage enzyme induces bacterial metabolic perturbation that confers a novel promiscuous function