Cloning and characterisation of the Neisseria gonorrhoeaearoB gene

  title={Cloning and characterisation of the Neisseria gonorrhoeaearoB gene},
  author={Roland Barten and Thomas F. Meyer},
  journal={Molecular and General Genetics MGG},
Abstract The gene coding for the 3-dehydroquinate synthetase (aroB) of Neisseria gonorrhoeae has been cloned by functional complementation of an Escherichia coli aroB mutant. The aroB gene isolated from a gonococcal plasmid library encodes a 359 amino acid protein with a molecular mass of 38.6 kDa. Alignment of different prokaryotic and eukaryotic aroB gene products reveals an overall identity ranging from 33 to 55%. An open reading frame coding for an aroK homologue is located immediately… 
Cloning and analysis of the aroB gene encoding dehydroquinate synthase from Corynebacterium glutamicum.
Alignment of different prokaryotic and eukaryotic aroB gene products reveals an overall identity ranging from 29 to 57% and the presence of several highly conserved regions.
Deletion of porA by Recombination between Clusters of Repetitive Extragenic Palindromic Sequences in Neisseria meningitidis
ABSTRACT PorA is an important component in a vaccine against infection withNeisseria meningitidis. However, porA-negative meningococci were isolated from patients, thereby potentially limiting the
The highly conserved domain of unknown function 1792 has a distinct glycosyltransferase fold
A 1.34 Å resolution X-ray crystallographic structure of a previously uncharacterized “domain of unknown function” 1792 (DUF1792) is reported and it is shown that the domain adopts a new fold and is required for glycosylation of a family of serine-rich repeat streptococcal adhesins.
Structure of the Ergothioneine‐Biosynthesis Amidohydrolase EgtC
The crystal structure of EgtC is determined from Mycobacterium smegmatis in complex with its physiological substrate and the set of active site residues that define substrate specificity in Egt C are highly conserved, even in homologues that are not involved in ergothioneine production.
The biosynthesis of shikimate metabolites.
  • A. Knaggs
  • Biology, Chemistry
    Natural product reports
  • 2001
This review covers the literature published during 2000 on the biosynthesis of compounds derived wholly or partly from intermediates on the shikimate pathway, including pyrrolnitrin, violacein, indole-3-acetic acid, coumarins, lignanoids, ubiquin one, TOPA quinone, PQQ, and tropanes.


Novel determinant (comA) essential for natural transformation competence in Neisseria gonorrhoeae and the effect of a comA defect on pilin variation
Only one of two open reading frames identified in comA is essential for competence: it encodes a protein (ComA) with a predicted size of 74kDa, in agreement with previous observations supporting the notion that multiple recombination pathways contribute to the variability of pilE.
Porin protein of Neisseria gonorrhoeae: cloning and gene structure.
The outer membrane porin molecule of Neisseria gonorrhoeae is known as protein I (PI). Among different strains of gonococci there is variability of PI, and two main classes, PIA and PIB, have been
Neisseria gonorrhoeae strain MS11 harbouring a mutation in gene aroA is attenuated and immunogenic.
This is the first demonstration of attenuation of Neisseria gonorrhoeae by introduction of a defined mutation in a metabolic gene as detected by ELISA using whole sonicated gonococci.
The product of the pilQ gene is essential for the biogenesis of type IV pili in Neisseria gonorrhoeae
PilQ is proposed to function in the terminal steps of organelle biogenesis by acting as a pilus channel or pore in Pseudomonas aeruginosa by virtue of their expression of rare pilus filaments.
An aroA mutant of Yersinia pestis is attenuated in guinea-pigs, but virulent in mice.
Unusually for an aro-defective mutant, the Y. pestis aroA mutant was virulent in mice, with a median dose which induced morbidity of death similar to that of the wild-type, although time to death was significantly prolonged.
Mecillinam resistance in Escherichia coli is conferred by loss of a second activity of the AroK protein
The ability of the aroK mutation to confer mecillinam resistance is shown to be independent of polar effects on operon expression and of effects on the availability of aromatic amino acids or shikimic acid.
Identification of the gene (aroK) encoding shikimic acid kinase I of Escherichia coli
It is proposed that urf1 encodes shikimate kinase I and that it be designated aroK, indicating that these two genes constitute a transcriptional unit with a polar effect on aroB.
Dehydroquinate synthase from Escherichia coli: purification, cloning, and construction of overproducers of the enzyme.
The chromosomal enzyme from E. coli K-12, the cloned enzyme encoded by the plasmid pLC29-47, and the subcloned inducible enzymes encoded by pJB14 all comigrate on polyacrylamide gel electrophoresis under denaturing conditions.
Identification and arrangement of the DNA sequence recognized in specific transformation of Neisseria gonorrhoeae.
  • S. Goodman, J. J. Scocca
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1988
It is concluded that the signal for recognition of transforming DNA by gonococci is a frequent component of transcriptional terminator sequences and might account for the origin and maintenance of recognition sequences in the chromosomes of Gram-negative transformable bacteria.