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Pilin expression and processing in pilus mutants of Neisseria gonorrhoeae : critical role of Gly -1 in assembly
dc.contributor.authorKoomey, Michaelen_US
dc.contributor.authorBergstrom, S.en_US
dc.contributor.authorBlake, M.en_US
dc.contributor.authorSwanson, J.en_US
dc.date.accessioned2010-06-01T21:55:02Z
dc.date.available2010-06-01T21:55:02Z
dc.date.issued1991-02en_US
dc.identifier.citationKoomey, M.; Bergstrom, S.; Blake, M.; Swanson, J. (1991). "Pilin expression and processing in pilus mutants of Neisseria gonorrhoeae : critical role of Gly -1 in assembly." Molecular Microbiology 5(2): 279-287. <http://hdl.handle.net/2027.42/74951>en_US
dc.identifier.issn0950-382Xen_US
dc.identifier.issn1365-2958en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/74951
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=1674976&dopt=citationen_US
dc.description.abstractSpontaneous 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.en_US
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dc.format.extent3109 bytes
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dc.publisherBlackwell Publishing Ltden_US
dc.rights1991 Blackwell Publishingen_US
dc.titlePilin expression and processing in pilus mutants of Neisseria gonorrhoeae : critical role of Gly -1 in assemblyen_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelMicrobiology and Immunologyen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Microbiology and Immunology, The University of Michigan Medical School, Ann Arbor, Michigan 48109-0402, USA.en_US
dc.contributor.affiliationotherLaboratory of Bacteriology and Immunology, The Rockefeller University, New York, 10021, USA.en_US
dc.contributor.affiliationotherDepartment of Microbiology, University of Umea, S-90187, Umea, Sweden.en_US
dc.contributor.affiliationotherDepartment of Health and Human Services, National Institute of Health, National Institutes of Allergy and Infectious Diseases, Laboratory of Microbial Structure and Function, Rocky Mountain Laboratories, Hamilton, Montana 59840, USA.en_US
dc.identifier.pmid1674976en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/74951/1/j.1365-2958.1991.tb02108.x.pdf
dc.identifier.doi10.1111/j.1365-2958.1991.tb02108.xen_US
dc.identifier.sourceMolecular Microbiologyen_US
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dc.owningcollnameInterdisciplinary and Peer-Reviewed


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