PXD043900

PXD043900 is an original dataset announced via ProteomeXchange.

Title	The previously uncharacterized YlxR (RnpM) protein modulates the activity of ribonuclease P
Description	Even though Bacillus subtilis is one of the most studied organisms, no function has been identified for about 20% of its proteins. Among these unknown proteins are several RNA- and ribosome-binding proteins suggesting that they exert functions in cellular information processing. In this work, we have investigated the RNA-binding protein YlxR. This protein is widely conserved in bacteria and strongly constitutively expressed in B. subtilis suggesting an important function. We have identified the RNA subunit of the essential RNase P as the binding partner of YlxR. The main activity of RNase P is the processing of 5’ ends of pre-tRNAs. In vitro processing assays demonstrated that the presence of YlxR results in reduced RNase P activity. Chemical cross-linking studies followed by in silico docking analysis and experiments with site-directed mutant proteins suggest that YlxR binds to the region of the RNase P RNA that is important for binding and cleavage of the pre-tRNA substrate. We conclude that the YlxR protein is a check protein that serves to limit RNase P activity to ensure appropriate amounts of mature tRNAs for translation. We rename the YlxR protein RnpM for RNase P modulator.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_06:45:35.633.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Aleksandar Chernev
SpeciesList	scientific name: Bacillus subtilis; NCBI TaxID: 1423;
ModificationList	monohydroxylated residue
Instrument	Orbitrap Exploris 480

Revision	Datetime	Status	ChangeLog Entry
0	2023-07-19 03:40:42	ID requested
1	2024-06-16 01:10:47	announced
⏵ 2	2024-10-22 06:45:36	announced	2024-10-22: Updated project metadata.

10.1093/nar/gkad1171;

Wicke D, Neumann P, G, ö, ß, ringer M, Chernev A, Davydov S, Poehlein A, Daniel R, Urlaub H, Hartmann RK, Ficner R, St, ü, lke J, The previously uncharacterized RnpM (YlxR) protein modulates the activity of ribonuclease P in Bacillus subtilis in vitro. Nucleic Acids Res, 52(3):1404-1419(2024) [pubmed]

submitter keyword: Bacillus subtilis,protein-RNA crosslinking

Henning Urlaub
contact affiliation	Max-Planck-Institute for Multidisciplinary Sciences Bioanalytical Mass Spectrometry Group Am Fassberg 11 D-37077 Goettingen, Germany University Medical Center Goettingen Bioanalytics Institute for Clinical Chemistry Robert Koch Strasse 40 D-37075 Goettingen, Germany
contact email	henning.urlaub@mpinat.mpg.de
lab head
Aleksandar Chernev
contact affiliation	MPIbpc
contact email	aleksandar.chernev@mpibpc.mpg.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD043900
     1. Label: PRIDE project
     2. Name: The previously uncharacterized YlxR (RnpM) protein modulates the activity of ribonuclease P