Only One of the Five CheY Homologs in <i>Vibrio cholerae</i> Directly Switches Flagellar Rotation
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- Akihiro Hyakutake
- Division of Biological Science, Graduate School of Science
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- Michio Homma
- Division of Biological Science, Graduate School of Science
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- Melissa J. Austin
- Department of Microbiology, Oregon State University, 220 Nash Hall, Corvallis, Oregon 97331
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- Markus A. Boin
- Department of Microbiology, Oregon State University, 220 Nash Hall, Corvallis, Oregon 97331
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- Claudia C. Häse
- Department of Microbiology, Oregon State University, 220 Nash Hall, Corvallis, Oregon 97331
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- Ikuro Kawagishi
- Division of Biological Science, Graduate School of Science
抄録
<jats:title>ABSTRACT</jats:title> <jats:p> <jats:italic>Vibrio cholerae</jats:italic> has three sets of chemotaxis (Che) proteins, including three histidine kinases (CheA) and four response regulators (CheY) that are encoded by three <jats:italic>che</jats:italic> gene clusters. We deleted the <jats:italic>cheY</jats:italic> genes individually or in combination and found that only the <jats:italic>cheY3</jats:italic> deletion impaired chemotaxis, reinforcing the previous conclusion that <jats:italic>che</jats:italic> cluster II is involved in chemotaxis. However, this does not exclude the involvement of the other clusters in chemotaxis. In other bacteria, phospho-CheY binds directly to the flagellar motor to modulate its rotation, and CheY overexpression, even without CheA, causes extremely biased swimming behavior. We reasoned that a <jats:italic>V. cholerae</jats:italic> CheY homolog, if it directly controls flagellar rotation, should also induce extreme swimming behavior when overproduced. This was the case for CheY3 ( <jats:italic>che</jats:italic> cluster II). However, no other CheY homolog, including the putative CheY (CheY0) protein encoded outside the <jats:italic>che</jats:italic> clusters, affected swimming, demonstrating that these CheY homologs cannot act directly on the flagellar motor. CheY4 very slightly enhanced the spreading of an <jats:italic>Escherichia coli cheZ</jats:italic> mutant in semisolid agar, raising the possibility that it can affect chemotaxis by removing a phosphoryl group from CheY3. We also found that <jats:italic>V. cholerae</jats:italic> CheY3 and <jats:italic>E. coli</jats:italic> CheY are only partially exchangeable. Mutagenic analyses suggested that this may come from coevolution of the interacting pair of proteins, CheY and the motor protein FliM. Taken together, it is likely that the principal roles of <jats:italic>che</jats:italic> clusters I and III as well as <jats:italic>cheY0</jats:italic> are to control functions other than chemotaxis. </jats:p>
収録刊行物
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- Journal of Bacteriology
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Journal of Bacteriology 187 (24), 8403-8410, 2005-12-15
American Society for Microbiology
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詳細情報 詳細情報について
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- CRID
- 1360574095460018048
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- NII論文ID
- 30021053798
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- ISSN
- 10985530
- 00219193
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- データソース種別
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