期刊
JOURNAL OF BACTERIOLOGY
卷 190, 期 6, 页码 1912-1921出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.01421-07
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- NCRR NIH HHS [P20 RR15574, P20 RR015574] Funding Source: Medline
- NIAID NIH HHS [AI29743, R01 AI029743] Funding Source: Medline
- NIAMS NIH HHS [R03 AR050656] Funding Source: Medline
Borrelia burgdorferi is a flat-wave, motile spirochete that causes Lyme disease. Motility is provided by periplasmic flagella (PFs) located between the cell cylinder and an outer membrane sheath. The structure of these PFs, which are composed of a basal body, a hook, and a filament, is similar to the structure of flagella of other bacteria. To determine if hook formation influences flagellin gene transcription in B. burgdorferi, we inactivated the hook structural gene JIBE by targeted mutagenesis. In many bacteria, completion of the hook structure serves as a checkpoint for transcriptional control of flagellum synthesis and other chemotaxis and motility genes. Specifically, the hook allows secretion of the anti-sigma factor flgM and concomitant late gene transcription promoted by sigma(28). However, the control of B. burgdorferi PF synthesis differs from the control of flagellum synthesis in other bacteria; the gene encoding sigma(28) is not present in the genome of B. burgdorferi, nor are any sigma(28) promoter recognition sequences associated with the motility genes. We found that B. burgdorferi JIBE mutants lacked PFs, were rod shaped, and were nonmotile, which substantiates previous evidence that PFs are involved in both cell morphology and motility. Although most motility and chemotaxis gene products accumulated at wild-type levels in the absence of flgE, mutant cells had markedly decreased levels of the flagellar filament proteins flaA and FlaB. Further analyses showed that the reduction in the levels of flageilin proteins in the spirochetes lacking flgE was mediated at the posttranscriptional level. Taken together, our results indicate that in B. burgdorferi, the completion of the hook does not serve as a checkpoint for transcriptional regulation of flagellum synthesis. In addition, we also present evidence that the hook protein in B. burgdorferi forms a high-molecular-weight complex and that formation of this complex occurs in the periplasmic space.
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