ArticleNucleic acids research2012
Opposing effects of DNA on proteolysis of a replication initiator.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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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.
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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.
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Who cites it
20 citing papers in PubMed, 30 citations in OpenAlex.
- PolyP inhibits CobB deacetylase triggering a regulatory coupling to prevent DNA replication initiation.Nucleic acids research · 2026Article
- Concise Overview of Methodologies Employed in the Study of Bacterial DNA Replication.International journal of molecular sciences · 2025Review
- Advancing evolution: Bacteria break down gene silencer to express horizontally acquired genes.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- G-quadruplexes rescuing protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- ClpC2 protects mycobacteria against a natural antibiotic targeting ClpC1-dependent protein degradation.Communications biology · 2023Article
- Bacterial hydrophilins promote pathogen desiccation tolerance.Cell host & microbe · 2022Article
- Mechanisms of Theta Plasmid Replication in Enterobacteria and Implications for Adaptation to Its Host.EcoSal Plus · 2020Review
- Polyphosphate induces the proteolysis of ADP-bound fraction of initiator to inhibit DNA replication initiation upon stress in Escherichia coli.Nucleic acids research · 2020Article
- DNA and Polyphosphate in Directed Proteolysis for DNA Replication Control.Frontiers in microbiology · 2020Review
- ClpAP protease is a universal factor that activates the parDE toxin-antitoxin system from a broad host range RK2 plasmid.Scientific reports · 2018Article
- Regulated Proteolysis in Bacteria.Annual review of biochemistry · 2018Review
- Temporal Proteomics of Inducible RNAi Lines of Clp Protease Subunits Identifies Putative Protease Substrates.Plant physiology · 2018Article
- Defining the crucial domain and amino acid residues in bacterial Lon protease for DNA binding and processing of DNA-interacting substrates.The Journal of biological chemistry · 2017Article
- Handcuffing reversal is facilitated by proteases and replication initiator monomers.Nucleic acids research · 2017Article
- Plasmid replication initiator interactions with origin 13-mers and polymerase subunits contribute to strand-specific replisome assembly.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The ClpXP protease is responsible for the degradation of the Epsilon antidote to the Zeta toxin of the streptococcal pSM19035 plasmid.The Journal of biological chemistry · 2014Article
- Review
- Roles of long and short replication initiation proteins in the fate of IncP-1 plasmids.Journal of bacteriology · 2012Article
- Polyphosphate, cyclic AMP, guanosine tetraphosphate, and c-di-GMP reduce in vitro Lon activity.BioengineeredArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DNA replication initiation proteins (Reps) are subjected to degradation by cellular proteases. We investigated how the formation of nucleoprotein complex, involving Rep and a protease, affects Rep degradation. All known Escherichia coli AAA+ cytosolic proteases and the replication initiation protein TrfA of the broad-host-range plasmid RK2 were used. Our results revealed that DNA influences the degradation process and that the observed effects are opposite and protease specific. In the case of ClpXP and ClpYQ proteases, DNA abolishes proteolysis, while in the case of ClpAP and Lon proteases it stimulates the process. ClpX and ClpY cannot interact with DNA-bound TrfA, while the ClpAP and Lon activities are enhanced by the formation of nucleoprotein complexes involving both the protease and TrfA. Lon has to interact with TrfA before contacting DNA, or this interaction can occur with TrfA already bound to DNA. The TrfA degradation by Lon can be carried out only on DNA. The absence of Lon results with higher stability of TrfA in the cell.
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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.