ArticleThe Journal of biological chemistry2015
Interaction with Single-stranded DNA-binding Protein Stimulates Escherichia coli Ribonuclease HI Enzymatic Activity.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 73 citations in OpenAlex.
- Single-molecule tracking of RNA-DNA hybrid removal enzymes important for lagging-strand replication.Biophysical journal · 2026Article
- Single-molecule tracking of RNA-DNA hybrid removal enzymes important for lagging-strand replication.bioRxiv : the preprint server for biology · 2025Article
- RPA transforms RNase H1 to a bidirectional exoribonuclease for processive RNA-DNA hybrid cleavage.Nature communications · 2024Article
- Escherichia coli DNA replication: the old model organism still holds many surprises.FEMS microbiology reviews · 2024Review
- The intrinsically disordered linker in the single-stranded DNA-binding protein influences DNA replication restart and recombination pathways inJournal of bacteriology · 2024Article
- Interaction with the carboxy-terminal tip of SSB is critical for RecG function in E. coli.Nucleic acids research · 2023Article
- Strand specificity of ribonucleotide excision repair in Escherichia coli.Nucleic acids research · 2023Article
- The Escherichia coli clamp loader rapidly remodels SSB on DNA to load clamps.Nucleic acids research · 2022Article
- The Impact of RNA-DNA Hybrids on Genome Integrity in Bacteria.Annual review of microbiology · 2022Review
- NAT10 and DDX21 Proteins Interact with RNase H1 and Affect the Performance of Phosphorothioate Oligonucleotides.Nucleic acid therapeutics · 2022Article
- RNase H is an exo- and endoribonuclease with asymmetric directionality, depending on the binding mode to the structural variants of RNA:DNA hybrids.Nucleic acids research · 2022Article
- Complete genome sequencing of aFrontiers in microbiology · 2022Article
- The mechanism of action of the SSB interactome reveals it is the first OB-fold family of genome guardians in prokaryotes.Protein science : a publication of the Protein Society · 2021Review
- Alternative complexes formed by the Escherichia coli clamp loader accessory protein HolC (x) with replication protein HolD (ψ) and repair protein YoaA.DNA repair · 2021Article
- Best practices for the visualization, mapping, and manipulation of R-loops.The EMBO journal · 2021Review
- Mutational Analysis of Residues in PriA and PriC Affecting Their Ability To Interact with SSB in Escherichia coli K-12.Journal of bacteriology · 2020Article
- A second hybrid-binding domain modulates the activity of Drosophila ribonuclease H1.Journal of biochemistry · 2020Article
- Interaction with single-stranded DNA-binding protein localizes ribonuclease HI to DNA replication forks and facilitates R-loop removal.Molecular microbiology · 2020Article
- Development of a single-stranded DNA-binding protein fluorescent fusion toolbox.Nucleic acids research · 2020Article
- The mechanism of Single strand binding protein-RecG binding: Implications for SSB interactome function.Protein science : a publication of the Protein Society · 2020Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Single-stranded (ss) DNA-binding proteins (SSBs) bind and protect ssDNA intermediates formed during replication, recombination, and repair reactions. SSBs also directly interact with many different genome maintenance proteins to stimulate their enzymatic activities and/or mediate their proper cellular localization. We have identified an interaction formed between Escherichia coli SSB and ribonuclease HI (RNase HI), an enzyme that hydrolyzes RNA in RNA/DNA hybrids. The RNase HI·SSB complex forms by RNase HI binding the intrinsically disordered C terminus of SSB (SSB-Ct), a mode of interaction that is shared among all SSB interaction partners examined to date. Residues that comprise the SSB-Ct binding site are conserved among bacterial RNase HI enzymes, suggesting that RNase HI·SSB complexes are present in many bacterial species and that retaining the interaction is important for its cellular function. A steady-state kinetic analysis shows that interaction with SSB stimulates RNase HI activity by lowering the reaction Km. SSB or RNase HI protein variants that disrupt complex formation nullify this effect. Collectively our findings identify a direct RNase HI/SSB interaction that could play a role in targeting RNase HI activity to RNA/DNA hybrid substrates within the genome.
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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.