ArticleBMC microbiology2009
Characterization of the meningococcal DNA glycosylase Fpg involved in base excision repair.
Article in BMC microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- The BER necessities: the repair of DNA damage in human-adapted bacterial pathogens.Nature reviews. Microbiology · 2015Review
- The Inner Membrane Protein PilG Interacts with DNA and the Secretin PilQ in Transformation.PloS one · 2015Article
- Mathematical and live meningococcal models for simple sequence repeat dynamics - coherent predictions and observations.PloS one · 2014Article
- A network of enzymes involved in repair of oxidative DNA damage in Neisseria meningitidis.Molecular microbiology · 2012Article
- Specialization of an Exonuclease III family enzyme in the repair of 3' DNA lesions during base excision repair in the human pathogen Neisseria meningitidis.Nucleic acids research · 2012Article
- Structure-function relationships of the competence lipoprotein ComL and SSB in meningococcal transformation.Microbiology (Reading, England) · 2011Article
- Mismatch correction modulates mutation frequency and pilus phase and antigenic variation in Neisseria gonorrhoeae.Journal of bacteriology · 2010Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundNeisseria meningitidis, the causative agent of meningococcal disease, is exposed to high levels of reactive oxygen species inside its exclusive human host. The DNA glycosylase Fpg of the base excision repair pathway (BER) is a central player in the correction of oxidative DNA damage. This study aimed at characterizing the meningococcal Fpg and its role in DNA repair.
resultsThe deduced N. meningitidis Fpg amino acid sequence was highly homologous to other Fpg orthologues, with particularly high conservation of functional domains. As for most N. meningitidis DNA repair genes, the fpg gene contained a DNA uptake sequence mediating efficient transformation of DNA. The recombinant N. meningitidis Fpg protein was over-expressed, purified to homogeneity and assessed for enzymatic activity. N. meningitidis Fpg was found to remove 2,6-diamino-4-hydroxy-5-formamidopyrimidine (faPy) lesions and 7,8-dihydro-8-oxo-2'-deoxyguanosine (8oxoG) opposite of C, T and G and to a lesser extent opposite of A. Moreover, the N. meningitidis fpg single mutant was only slightly affected in terms of an increase in the frequency of phase variation as compared to a mismatch repair mutant.
conclusionCollectively, these findings show that meningococcal Fpg functions are similar to those of prototype Fpg orthologues in other bacterial species.
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