ArticleBioMed research international2014
Rapid degradation of Hfq-free RyhB in Yersinia pestis by PNPase independent of putative ribonucleolytic complexes.
Article in BioMed research international, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- Regulation of mRNA Stability During Bacterial Stress Responses.Frontiers in microbiology · 2020Review
- Rewiring the functional complexity between Crc, Hfq and sRNAs to regulate carbon catabolite repression in Pseudomonas.World journal of microbiology & biotechnology · 2019Review
- RNA-Dependent Regulation of Virulence in Pathogenic Bacteria.Frontiers in cellular and infection microbiology · 2019Review
- Regulatory RNAs in Virulence and Host-Microbe Interactions.Microbiology spectrum · 2018Review
- Discovering RNA-Based Regulatory Systems forFrontiers in cellular and infection microbiology · 2018Review
- RNA-based mechanisms of virulence control in Enterobacteriaceae.RNA biology · 2017Review
- Tissue dual RNA-seq allows fast discovery of infection-specific functions and riboregulators shaping host-pathogen transcriptomes.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Analyzing the Complex Regulatory Landscape of Hfq - an Integrative, Multi-Omics Approach.Frontiers in microbiology · 2017Article
- Environmental Regulation of Yersinia Pathophysiology.Frontiers in cellular and infection microbiology · 2016Review
- Yersinia pestis and Yersinia pseudotuberculosis infection: a regulatory RNA perspective.Frontiers in microbiology · 2015Review
- Coregulation of host-adapted metabolism and virulence by pathogenic yersiniae.Frontiers in cellular and infection microbiology · 2014Review
- HmsB enhances biofilm formation in Yersinia pestis.Frontiers in microbiology · 2014Article
- Sibling rivalry: related bacterial small RNAs and their redundant and non-redundant roles.Frontiers in cellular and infection microbiology · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The RNA chaperone Hfq in bacteria stabilizes sRNAs by protecting them from the attack of ribonucleases. Upon release from Hfq, sRNAs are preferably degraded by PNPase. PNPase usually forms multienzyme ribonucleolytic complexes with endoribonuclease E and/or RNA helicase RhlB to facilitate the degradation of the structured RNA. However, whether PNPase activity on Hfq-free sRNAs is associated with the assembly of RNase E or RhlB has yet to be determined. Here we examined the roles of the main endoribonucleases, exoribonucleases, and ancillary RNA-modifying enzymes in the degradation of Y. pestis RyhB in the absence of Hfq. Expectedly, the transcript levels of both RyhB1 and RyhB2 increase only after inactivating PNPase, which confirms the importance of PNPase in sRNA degradation. By contrast, the signal of RyhB becomes barely perceptible after inactivating of RNase III, which may be explained by the increase in PNPase levels resulting from the exemption of pnp mRNA from RNase III processing. No significant changes are observed in RyhB stability after deletion of either the PNPase-binding domain of RNase E or rhlB. Therefore, PNPase acts as a major enzyme of RyhB degradation independent of PNPase-containing RNase E and RhlB assembly in the absence of Hfq.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.