ArticleProceedings of the National Academy of Sciences of the United States of America2005
RhlB helicase rather than enolase is the beta-subunit of the Escherichia coli polynucleotide phosphorylase (PNPase)-exoribonucleolytic complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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35 citing papers in PubMed, 68 citations in OpenAlex.
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- RNA exoribonucleases in E. coli.Archives of microbiology · 2026Review
- How hydrolytic exoribonucleases impact human disease: Two sides of the same story.FEBS open bio · 2023Review
- PNPase and RhlB Interact and Reduce the Cellular Availability of Oxidized RNA inMicrobiology spectrum · 2022Article
- Dimeric assembly of human Suv3 helicase promotes its RNA unwinding function in mitochondrial RNA degradosome for RNA decay.Protein science : a publication of the Protein Society · 2022Article
- Review
- Regulation of mRNA decay inCritical reviews in biochemistry and molecular biology · 2022Article
- Activity and Function in Human Cells of the Evolutionary Conserved Exonuclease Polynucleotide Phosphorylase.International journal of molecular sciences · 2022Review
- The world of ribonucleases from pseudomonads: a short trip through the main features and singularities.Microbial biotechnology · 2021Review
- Posttranscriptional Regulation ofJournal of bacteriology · 2020Article
- The Bacterial Counterparts of the Eukaryotic Exosome: An Evolutionary Perspective.Methods in molecular biology (Clifton, N.J.) · 2020Review
- Bacterial ribonucleases and their roles in RNA metabolism.Critical reviews in biochemistry and molecular biology · 2019Review
- Role of ribosome assembly in Escherichia coli ribosomal RNA degradation.Nucleic acids research · 2018Article
- Polynucleotide phosphorylase: Not merely an RNase but a pivotal post-transcriptional regulator.PLoS genetics · 2018Review
- Enzymes Involved in Posttranscriptional RNA Metabolism in Gram-Negative Bacteria.Microbiology spectrum · 2018Review
- Inhibition of homologous phosphorolytic ribonucleases by citrate may represent an evolutionarily conserved communicative link between RNA degradation and central metabolism.Nucleic acids research · 2017Article
- Helicase Activity Plays a Crucial Role for RNase R Function in Vivo and for RNA Metabolism.The Journal of biological chemistry · 2016Article
- How RNase R Degrades Structured RNA: ROLE OF THE HELICASE ACTIVITY AND THE S1 DOMAIN.The Journal of biological chemistry · 2016Article
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2 authors at 1 institution in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli polynucleotide phosphorylase (PNPase), a protein that has both ribonucleolytic and synthetic capabilities, binds, along with the 48-kDa glycolytic enzyme enolase, the 50-kDa DEAD-box protein RhlB helicase and other cellular proteins to the C-terminal "scaffold" region of RNase E to form a complex termed the RNA degradosome. PNPase itself has been reported to exist as a complex (alpha(3)beta(2)) containing trimers of a catalytic subunit (alpha) and dimers of another subunit (beta). The beta-subunit has been believed to be enolase; we report here that it is instead the RhlB helicase. Whereas interaction between PNPase-alpha and enolase was observed in bacteria that synthesize RNase E having a scaffold region, immunoprecipitates from cells expressing PNPase-alpha, RhlB, and enolase from single-copy chromosomal loci, plus a mutant RNase E protein lacking its C-terminal half, showed direct association of PNPase-alpha only with RhlB. Using affinity chromatography, we found that PNPase-alpha and RhlB form a ribonucleolytically active complex corresponding to the mass calculated previously for alpha(3)beta(2) (i.e., 377-380 kDa), whereas no association between PNPase-alpha and enolase was detected. Chromosomal deletion of the eno gene had no effect on the ability of PNPase to degrade either single- or double-stranded RNAs. Collectively, our findings show that direct interaction between PNPase-alpha and RhlB occurs physiologically in the absence of the RNase E C-terminal region, that enolase association with PNPase-alpha is a consequence of the interaction of both proteins with RNase E, and that, contrary to current notions, enolase is not the beta-subunit of E. coli PNPase complex.
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