Abstract:
:Spirochetes have a unique motility system that is characterized by flagellar filaments contained within the outer membrane sheath. Direct evidence using video microscopy has recently been obtained which indicates that these periplasmic flagella (PF) rotate in several spirochetal species. This rotation generates thrust. As shown for one spirochete, Spirochaeta aurantia, motility is driven by a proton motive force. Spirochete chemotaxis has been most thoroughly studied in S. aurantia. This spirochete exhibits three distinct behaviours, runs of smooth swimming, reversals and flexing. These behaviours are modulated by addition of attractants such that S. aurantia swims towards higher concentrations of attractants in a spatial gradient. Unlike the prototypical bacterium, Escherichia coli, chemotaxis in S. aurantia involves fluctuations in membrane potential. The PF of a number of spirochetes have been examined in considerable detail. For most species, the PF filaments are complex, consisting of an assembly of several different polypeptides. There are several antigenically related core polypeptides surrounded by an outer layer consisting of a different polypeptide. Borrelia burgdorferi and Spirochaeta zuelzerae represent exceptions where the filaments are composed of a single major polypeptide species. The genes encoding the filament polypeptides from several spirochete species have been cloned and analysed. Apparently, the outer layer polypeptides of S. aurantia, Treponema pallidum and Serpulina hyodysenteriae are transcribed from sigma-70-like promoters, whereas the core polypeptide genes are transcribed from sigma-28-like promoters. A gene encoding the hook polypeptide in Treponema phagedenis has been cloned and analysed. The product of this gene shows significant similarity to the E. coli hook protein, FlgE, and homologs have been identified in T. pallidum and B. burgdorferi.(ABSTRACT TRUNCATED AT 250 WORDS)
journal_name
Res Microbioljournal_title
Research in microbiologyauthors
Charon NW,Greenberg EP,Koopman MB,Limberger RJdoi
10.1016/0923-2508(92)90117-7subject
Has Abstractpub_date
1992-07-01 00:00:00pages
597-603issue
6eissn
0923-2508issn
1769-7123pii
0923-2508(92)90117-7journal_volume
143pub_type
杂志文章,评审abstract::The Escherichia coli mannitol permease (EIIMtl) of the phosphoenolpyruvate-dependent phosphotransferase system is a 68-kDa membrane protein that carries out the concomitant transport and phosphorylation of D-mannitol. Previous studies indicated that there are ca. 6 membrane-spanning helices within the N-terminal half ...
journal_title:Research in microbiology
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journal_title:Research in microbiology
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journal_title:Research in microbiology
pub_type: 杂志文章,评审
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journal_title:Research in microbiology
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journal_title:Research in microbiology
pub_type: 杂志文章
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journal_title:Research in microbiology
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