ArticleJournal of bacteriology2004
The RecA protein of Helicobacter pylori requires a posttranslational modification for full activity.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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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Who cites it
24 citing papers in PubMed, 48 citations in OpenAlex.
- Reinvestigation into the role of lipopolysaccharide Glycosyltransferases inGut microbes · 2025Article
- Identification of Streptococcus mitis321A vaccine antigens based on reverse vaccinology.Molecular medicine reports · 2018Article
- Survival of Helicobacter pylori in gastric acidic territory.Helicobacter · 2017Review
- Helicobacter pylori strains from a Nigerian cohort show divergent antibiotic resistance rates and a uniform pathogenicity profile.PloS one · 2017Article
- The CagA toxin of Helicobacter pylori: abundant production but relatively low amount translocated.Scientific reports · 2016Article
- The BER necessities: the repair of DNA damage in human-adapted bacterial pathogens.Nature reviews. Microbiology · 2015Review
- The sweet tooth of bacteria: common themes in bacterial glycoconjugates.Microbiology and molecular biology reviews : MMBR · 2014Review
- Structural insights into the unique single-stranded DNA-binding mode of Helicobacter pylori DprA.Nucleic acids research · 2014Article
- Intracellular locations of replication proteins and the origin of replication during chromosome duplication in the slowly growing human pathogen Helicobacter pylori.Journal of bacteriology · 2014Article
- CagI is an essential component of the Helicobacter pylori Cag type IV secretion system and forms a complex with CagL.PloS one · 2012Article
- Biochemical and cellular characterization of Helicobacter pylori RecA, a protein with high-level constitutive expression.Journal of bacteriology · 2011Article
- Change is good: variations in common biological mechanisms in the epsilonproteobacterial genera Campylobacter and Helicobacter.Microbiology and molecular biology reviews : MMBR · 2011Review
- Article
- Recombination and DNA repair in Helicobacter pylori.Annual review of microbiology · 2011Review
- Complexomics study of two Helicobacter pylori strains of two pathological origins: potential targets for vaccine development and new insight in bacteria metabolism.Molecular & cellular proteomics : MCP · 2010Article
- The coupling protein Cagbeta and its interaction partner CagZ are required for type IV secretion of the Helicobacter pylori CagA protein.Infection and immunity · 2010Article
- Strain-specific genes of Helicobacter pylori: genome evolution driven by a novel type IV secretion system and genomic island transfer.Nucleic acids research · 2010Article
- A cytoplasmic prolyl hydroxylation and glycosylation pathway modifies Skp1 and regulates O2-dependent development in Dictyostelium.Biochimica et biophysica acta · 2010Review
- Dual nuclease and helicase activities of Helicobacter pylori AddAB are required for DNA repair, recombination, and mouse infectivity.The Journal of biological chemistry · 2009Article
- A RecB-like helicase in Helicobacter pylori is important for DNA repair and host colonization.Infection and immunity · 2009Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The RecA protein is a central component of the homologous recombination machinery and of the SOS system in most bacteria. In performing these functions, it is involved in DNA repair processes and plays an important role in natural transformation competence. This may be especially important in Helicobacter pylori, where an unusually high degree of microdiversity among strains is generated by homologous recombination. We have suggested previously that the H. pylori RecA protein is subject to posttranslational modifications that result in a slight shift in its electrophoretic mobility. Here we show that at least two genes downstream of recA are involved in this modification and that this process is dependent on genes involved in glycosylation and lipopolysaccharide biosynthesis. Site-directed mutagenesis of a putative glycosylation site results in production of an unmodified RecA protein. This posttranslational modification is not involved in membrane targeting or cell division functions but is necessary for the full function of RecA in DNA repair. Thus, it might be an adaptation to the specific requirements of H. pylori in its natural environment.
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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.