author_facet Ge, Y
Charon, N W
Ge, Y
Charon, N W
author Ge, Y
Charon, N W
spellingShingle Ge, Y
Charon, N W
Journal of Bacteriology
An unexpected flaA homolog is present and expressed in Borrelia burgdorferi
Molecular Biology
Microbiology
author_sort ge, y
spelling Ge, Y Charon, N W 0021-9193 1098-5530 American Society for Microbiology Molecular Biology Microbiology http://dx.doi.org/10.1128/jb.179.2.552-556.1997 <jats:p>Most investigators have assumed that the periplasmic flagella (PFs) of Borrelia burgdorferi are composed of only one flagellin protein. The PFs of most other spirochete species are complex: these PFs contain an outer sheath of FlaA proteins and a core filament of FlaB proteins. During an analysis of a chemotaxis gene cluster of B. burgdorferi 212, we were surprised to find a flaA gene homolog with a deduced polypeptide having 54 to 58% similarity to FlaA from other spirochetes. Like other FlaA proteins, B. burgdorferi FlaA has a conserved signal sequence at its N terminus. Based on reverse transcription-PCR and primer extension analysis, this flaA homolog and five chemotaxis genes constitute a motility-chemotaxis operon. Immunoblots using anti-FlaA serum from Treponema pallidum and a lysate of B. burgdorferi showed strong reactivity to a protein of 38.0 kDa, which is consistent with the expression of flaA in growing cells.</jats:p> An unexpected flaA homolog is present and expressed in Borrelia burgdorferi Journal of Bacteriology
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title An unexpected flaA homolog is present and expressed in Borrelia burgdorferi
title_unstemmed An unexpected flaA homolog is present and expressed in Borrelia burgdorferi
title_full An unexpected flaA homolog is present and expressed in Borrelia burgdorferi
title_fullStr An unexpected flaA homolog is present and expressed in Borrelia burgdorferi
title_full_unstemmed An unexpected flaA homolog is present and expressed in Borrelia burgdorferi
title_short An unexpected flaA homolog is present and expressed in Borrelia burgdorferi
title_sort an unexpected flaa homolog is present and expressed in borrelia burgdorferi
topic Molecular Biology
Microbiology
url http://dx.doi.org/10.1128/jb.179.2.552-556.1997
publishDate 1997
physical 552-556
description <jats:p>Most investigators have assumed that the periplasmic flagella (PFs) of Borrelia burgdorferi are composed of only one flagellin protein. The PFs of most other spirochete species are complex: these PFs contain an outer sheath of FlaA proteins and a core filament of FlaB proteins. During an analysis of a chemotaxis gene cluster of B. burgdorferi 212, we were surprised to find a flaA gene homolog with a deduced polypeptide having 54 to 58% similarity to FlaA from other spirochetes. Like other FlaA proteins, B. burgdorferi FlaA has a conserved signal sequence at its N terminus. Based on reverse transcription-PCR and primer extension analysis, this flaA homolog and five chemotaxis genes constitute a motility-chemotaxis operon. Immunoblots using anti-FlaA serum from Treponema pallidum and a lysate of B. burgdorferi showed strong reactivity to a protein of 38.0 kDa, which is consistent with the expression of flaA in growing cells.</jats:p>
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author Ge, Y, Charon, N W
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description <jats:p>Most investigators have assumed that the periplasmic flagella (PFs) of Borrelia burgdorferi are composed of only one flagellin protein. The PFs of most other spirochete species are complex: these PFs contain an outer sheath of FlaA proteins and a core filament of FlaB proteins. During an analysis of a chemotaxis gene cluster of B. burgdorferi 212, we were surprised to find a flaA gene homolog with a deduced polypeptide having 54 to 58% similarity to FlaA from other spirochetes. Like other FlaA proteins, B. burgdorferi FlaA has a conserved signal sequence at its N terminus. Based on reverse transcription-PCR and primer extension analysis, this flaA homolog and five chemotaxis genes constitute a motility-chemotaxis operon. Immunoblots using anti-FlaA serum from Treponema pallidum and a lysate of B. burgdorferi showed strong reactivity to a protein of 38.0 kDa, which is consistent with the expression of flaA in growing cells.</jats:p>
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spelling Ge, Y Charon, N W 0021-9193 1098-5530 American Society for Microbiology Molecular Biology Microbiology http://dx.doi.org/10.1128/jb.179.2.552-556.1997 <jats:p>Most investigators have assumed that the periplasmic flagella (PFs) of Borrelia burgdorferi are composed of only one flagellin protein. The PFs of most other spirochete species are complex: these PFs contain an outer sheath of FlaA proteins and a core filament of FlaB proteins. During an analysis of a chemotaxis gene cluster of B. burgdorferi 212, we were surprised to find a flaA gene homolog with a deduced polypeptide having 54 to 58% similarity to FlaA from other spirochetes. Like other FlaA proteins, B. burgdorferi FlaA has a conserved signal sequence at its N terminus. Based on reverse transcription-PCR and primer extension analysis, this flaA homolog and five chemotaxis genes constitute a motility-chemotaxis operon. Immunoblots using anti-FlaA serum from Treponema pallidum and a lysate of B. burgdorferi showed strong reactivity to a protein of 38.0 kDa, which is consistent with the expression of flaA in growing cells.</jats:p> An unexpected flaA homolog is present and expressed in Borrelia burgdorferi Journal of Bacteriology
spellingShingle Ge, Y, Charon, N W, Journal of Bacteriology, An unexpected flaA homolog is present and expressed in Borrelia burgdorferi, Molecular Biology, Microbiology
title An unexpected flaA homolog is present and expressed in Borrelia burgdorferi
title_full An unexpected flaA homolog is present and expressed in Borrelia burgdorferi
title_fullStr An unexpected flaA homolog is present and expressed in Borrelia burgdorferi
title_full_unstemmed An unexpected flaA homolog is present and expressed in Borrelia burgdorferi
title_short An unexpected flaA homolog is present and expressed in Borrelia burgdorferi
title_sort an unexpected flaa homolog is present and expressed in borrelia burgdorferi
title_unstemmed An unexpected flaA homolog is present and expressed in Borrelia burgdorferi
topic Molecular Biology, Microbiology
url http://dx.doi.org/10.1128/jb.179.2.552-556.1997