Pili of Neisseria gonorrhoeae undergo both phase and structural variation. Phase variation of gonococcal pili can be caused by a RecA-independent on/off switch in PilC, a protein involved in pilus biogenesis. We show here that spontaneous nonpiliated PilC- derivatives as well as PilC-insertional mutants have also acquired sequence alterations in pilE relative to the pilE gene of the piliated MS11mk(P+)-u parent, so that the pilin produced is processed to soluble S-pilin and can be released into the medium. It is proposed that pilin alterations are selected for in PilC-bacteria if the parental nonassembled pilin is toxic to the cells--i.e., is not degradable to S-pilin at rates sufficient to allow viability of the cells. Toxicity is indicated by the extreme instability of certain unassembled pilin sequences and by the low frequency of nonpiliated, pilin+, PilC- variants that emerge from piliated recA-cells. The presence of a point mutation changing leucine-39 to phenylalanine at the cleavage site for S-pilin in one nonpiliated, PilC-, recA-variant relative to its piliated parent is a further argument for a selective mechanism of structural diversity of the gonococcal pilin.
Subject | Predicate | Object | Context |
---|---|---|---|
http://purl.uniprot.org/cit... | rdf:type | uniprot:Journal_Citation | lld:uniprot |
http://purl.uniprot.org/cit... | rdfs:comment | Pili of Neisseria gonorrhoeae undergo both phase and structural variation. Phase variation of gonococcal pili can be caused by a RecA-independent on/off switch in PilC, a protein involved in pilus biogenesis. We show here that spontaneous nonpiliated PilC- derivatives as well as PilC-insertional mutants have also acquired sequence alterations in pilE relative to the pilE gene of the piliated MS11mk(P+)-u parent, so that the pilin produced is processed to soluble S-pilin and can be released into the medium. It is proposed that pilin alterations are selected for in PilC-bacteria if the parental nonassembled pilin is toxic to the cells--i.e., is not degradable to S-pilin at rates sufficient to allow viability of the cells. Toxicity is indicated by the extreme instability of certain unassembled pilin sequences and by the low frequency of nonpiliated, pilin+, PilC- variants that emerge from piliated recA-cells. The presence of a point mutation changing leucine-39 to phenylalanine at the cleavage site for S-pilin in one nonpiliated, PilC-, recA-variant relative to its piliated parent is a further argument for a selective mechanism of structural diversity of the gonococcal pilin. | lld:uniprot |
http://purl.uniprot.org/cit... | skos:exactMatch | http://purl.uniprot.org/med... | lld:uniprot |
http://purl.uniprot.org/cit... | skos:exactMatch | http://purl.uniprot.org/pub... | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:name | Proc. Natl. Acad. Sci. U.S.A. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:author | Normark S. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:author | Jonsson A.B. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:author | Pfeifer J. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:date | 1992 | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:pages | 3204-3208 | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:title | Neisseria gonorrhoeae PilC expression provides a selective mechanism for structural diversity of pili. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:volume | 89 | lld:uniprot |
http://purl.uniprot.org/cit... | dc-term:identifier | doi:10.1073/pnas.89.8.3204 | lld:uniprot |
uniprot-protein:P02974 | uniprot:citation | http://purl.uniprot.org/cit... | lld:uniprot |
http://purl.uniprot.org/SHA... | uniprot:citation | http://purl.uniprot.org/cit... | lld:uniprot |
http://linkedlifedata.com/r... | rdf:object | http://purl.uniprot.org/cit... | lld:uniprot |