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Pilus biogenesis gene, pilC, of Neisseria gonorrhoeae: pilC1 and pilC2 are each part of a larger duplication of the gonococcal genome and share upstream and downstream homologous sequences with opa and pil loci

Article Abstract:

The pilC1 gene, present in the MS11 strain of Neisseria gonorrhoeae, contains amino acid sequences similar to those present in the opa and pil gene locus. These amino acid sequences are repetitive in nature and are probably involved in recombination during the formation of pili, an antigen. The amino acid structure of pilC1 is 90% similar to that of pilC2 gene. The pilC1 gene is a part of the chromosome that encodes for pili and is formed by DNA duplication. Pili controls attachment of the bacterial cell to the host cell. The amino acid sequence of pilC1 is given.

Author: Normark, Staffan, Jonsson, Ann-Beth, Rahman, Motuir
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
Analysis, Antigens

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Glucosaminidase of Bacillus subtilis: cloning, regulation, primary structure and biochemical characterization

Article Abstract:

The glucosaminidase, produced by Bacillus subtilis AC327, is a 90 kDa protein containing direct repeats which are the cell wall binding regions. Loss of these repeats decreases the lytic ability of the protein. The lytD gene, encoding the protein, consists of a monocistronic operon containing a signal peptide. The lytD gene is expressed during the exponential growth phase and dissolves the bacterial cell wall of the cell expressing it. The expression of lytD decreases in the presence of a null mutation in sigD.

Author: Mori, Masao, Rashid, Muhammad H., Sekiguchi, Junichi
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
Bacillus subtilis, Proteins

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Involvement of the gonococcal MtrE protein in the resistance of Neisseria gonorrhoeae to toxic hydrophobic agents

Article Abstract:

The low-level resistance of Neisseria gonorrhoeae to toxic hydrophobic agents which includes some antibiotics was found chromosomally mediated by the multiple transferable resistance efflux system. The gene encoding the 48.3 kDa MtrE was observed homologous to export-associated pouter-membrane proteins which includes the OprM lipoprotein of Pseudomonas aeruginosa. An active efflux system was confirmed to mediate MtrE's role in multidrug resistance.

Author: Delahay, R.M., Robertson, B.D., Balthazar, J.T., Shafer, W.M., Ison, C.A.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
Antibiotics

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Subjects list: Research, Observations, Neisseria gonorrhoeae, Amino acid sequence, Amino acid sequencing
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