Characterization of the meningococcal DNA glycosylase Fpg involved in base excision repairReportar como inadecuado

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BMC Microbiology

, 9:7

First Online: 09 January 2009Received: 09 September 2008Accepted: 09 January 2009


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.

Electronic supplementary materialThe online version of this article doi:10.1186-1471-2180-9-7 contains supplementary material, which is available to authorized users.

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