ArticleThe Journal of biological chemistry2016
Interaction of Bacillus subtilis Polynucleotide Phosphorylase and RNase Y: STRUCTURAL MAPPING AND EFFECT ON mRNA TURNOVER.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Defining the networks that connect RNase III and RNase J-mediated regulation of primary and specialized metabolism inJournal of bacteriology · 2025Article
- Article
- Formation of a stable RNase Y-RicT (YaaT) complex requires RicA (YmcA) and RicF (YlbF).bioRxiv : the preprint server for biology · 2023Article
- Structural Insights into the Dimeric Form ofBiomolecules · 2022Article
- Article
- Single molecule/particle tracking analysis program SMTracker 2.0 reveals different dynamics of proteins within the RNA degradosome complex in Bacillus subtilis.Nucleic acids research · 2021Article
- Polynucleotide phosphorylase and RNA helicase CshA cooperate inRNA biology · 2021Article
- Quasi-essentiality of RNase Y in Bacillus subtilis is caused by its critical role in the control of mRNA homeostasis.Nucleic acids research · 2021Article
- Bacterial ribonucleases and their roles in RNA metabolism.Critical reviews in biochemistry and molecular biology · 2019Review
- Examining the Protein Interactome and Subcellular Localization of RNase J2 Complexes inFrontiers in microbiology · 2019Article
- Maturation of polycistronic mRNAs by the endoribonuclease RNase Y and its associated Y-complex inProceedings of the National Academy of Sciences of the United States of America · 2018Article
- RNases and Helicases in Gram-Positive Bacteria.Microbiology spectrum · 2018Article
- Localization of Components of the RNA-Degrading Machine inFrontiers in microbiology · 2016Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Polynucleotide phosphorylase (PNPase), a 3'-to-5' phosphorolytic exoribonuclease, is thought to be the primary enzyme responsible for turnover ofBacillus subtilismRNA. The role of PNPase inB. subtilismRNA decay has been analyzed previously by comparison of mRNA profiles in a wild-type strainversusa strain that is deleted forpnpA, the gene encoding PNPase. Recent studies have provided evidence for a degradosome-like complex inB. subtilisthat is built around the major decay-initiating endonuclease, RNase Y, and there is ample evidence for a strong interaction between PNPase and RNase Y. The role of the PNPase-RNase Y interaction in the exonucleolytic function of PNPase needs to be clarified. We sought to construct aB. subtilisstrain containing a catalytically active PNPase that could not interact with RNase Y. Mapping studies of the PNPase-RNase Y interaction were guided by a homology model ofB. subtilisPNPase based on the known structure of theEscherichia coliPNPase in complex with an RNase E peptide. Mutations inB. subtilisresidues predicted to be involved in RNase Y binding showed a loss of PNPase-RNase Y interaction. Two mRNAs whose decay is dependent on RNase Y and PNPase were examined in strains containing full-length PNPase that was either catalytically active but unable to interact with RNase Y, or catalytically inactive but able to interact with RNase Y. At least for these two mRNAs, disruption of the PNPase-RNase Y interaction did not appear to affect mRNA turnover.
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Registered trials
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