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Pilin expression and processing in pilus mutants of Neisseria gonorrhoeae : critical role of Gly ‐1 in assembly
Author(s) -
Koomey M.,
Bergstrom S.,
Blake M.,
Swanson J.
Publication year - 1991
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1991.tb02108.x
Subject(s) - pilin , pilus , biology , mutant , neisseria gonorrhoeae , fimbriae proteins , microbiology and biotechnology , genetics , escherichia coli , gene
Summary Spontaneous mutants of Neisseria gonorrheae failing to express pili or having diminished levels of piliation were studied with regard to pilin expression. All mutants displayed altered pilin processing detectable as the release of soluble, truncated pilin molecules (S‐pilin). Of particular interest was the finding, in one mutant, that substitution of serine for glycine at position ‐1 of propilin, a highly conserved residue among N ‐metPhe and related pilins, abolished pilus expression but not S‐pilin release. The degree of S‐pilin processing and the levels of membrane‐associated pilin varied among the different classes of mutants, suggesting that each was blocked at a distinct step of pilus biogenesis. The data support a model in which increased S‐pilin processing is a result of a decreased rate of pilus polymerization.