PXD018342

PXD018342 is an original dataset announced via ProteomeXchange.

Title	The leader peptide peTrpL forms antibiotic-containing ribonucleoprotein complexes for posttranscriptional regulation of multiresistance genes
Description	Bacterial ribosome-dependent attenuators are widespread posttranscriptional regulators. They harbour small upstream ORFs (uORFs) encoding leader peptides, for which no functions in trans are known yet. In the soil-dwelling plant symbiont Sinorhizobium meliloti, the tryptophan biosynthesis gene trpE(G) is preceded by the uORF trpL and is regulated by transcription attenuation according to tryptophan availability. However, trpLE(G) transcription is initiated independently of the tryptophan level in S. meliloti, thereby ensuring a largely tryptophan-independent production of the leader peptide peTrpL. Here we provide evidence for a tryptophan-independent role of peTrpL in trans. We found that peTrpL increases the resistance towards tetracycline, erythromycin, chloramphenicol and the flavonoid genistein, which are substrates of the major multidrug efflux pump SmeAB. Coimmunoprecipitation with 3×FLAG-peTrpL suggested smeR mRNA, which encodes the transcription repressor of smeABR, as a peptide target. Indeed, upon antibiotic exposure, smeR mRNA was destabilized and smeA stabilized in a peTrpL-dependent manner, showing that peTrpL acts in the differential regulation of smeABR. Further, smeR mRNA was coimmunoprecipitated with 3×FLAG-peTrpL in antibiotic-dependent ribonucleoprotein (ARNP) complexes, which in addition contained an antibiotic-induced antisense RNA complementary to smeR. In vitro ARNP reconstitution revealed that the above antibiotics and genistein directly support complex formation. A specific region of the antisense RNA was identified as a seed region for ARNP assembly in vitro. Altogether, our data show that peTrpL is involved in a mechanism for direct utilization of antimicrobial compounds in posttranscriptional regulation of multiresistance genes. We also show that the role of peTrpL in resistance is conserved in other Alphaproteobacteria
HostingRepository	PRIDE
AnnounceDate	2024-10-07
AnnouncementXML	Submission_2024-10-07_13:33:20.684.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Sandra Maass
SpeciesList	scientific name: Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti); NCBI TaxID: 382;
ModificationList	6x(13)C; 2xC(13),3x(2)H labeled N6-acetyl-L-lysine; monohydroxylated residue
Instrument	TSQ Vantage; LTQ Orbitrap

Revision	Datetime	Status	ChangeLog Entry
0	2020-04-03 00:14:53	ID requested
⏵ 1	2024-10-07 13:33:21	announced

Melior H, Maa, ß S, Li S, F, ö, rstner KU, Azarderakhsh S, Varadarajan AR, St, ö, tzel M, Elhossary M, Barth-Weber S, Ahrens CH, Becher D, Evguenieva-Hackenberg E, The Leader Peptide peTrpL Forms Antibiotic-Containing Ribonucleoprotein Complexes for Posttranscriptional Regulation of Multiresistance Genes. mBio, 11(3):(2020) [pubmed]

10.1128/mbio.01027-20;

submitter keyword: small proteins, posttranscriptional regulation, attenuator, multiresistance,Sinorhizobium meliloti, quantification

Dörte Becher
contact affiliation	University of Greifswald Institute of Microbiology Department of Microbial Proteomics Felix-Hausdorff-Str.8 17489 Greifswald
contact email	dbecher@uni-greifswald.de
lab head
Sandra Maass
contact affiliation	University of Greifswald, Department for Microbial Proteomics
contact email	sandra.maass@uni-greifswald.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD018342
     1. Label: PRIDE project
     2. Name: The leader peptide peTrpL forms antibiotic-containing ribonucleoprotein complexes for posttranscriptional regulation of multiresistance genes