ZomB is essential for flagellar motor reversals in Shewanella putrefaciens and Vibrio parahaemolyticus. Issue 5 (1st August 2018)
- Record Type:
- Journal Article
- Title:
- ZomB is essential for flagellar motor reversals in Shewanella putrefaciens and Vibrio parahaemolyticus. Issue 5 (1st August 2018)
- Main Title:
- ZomB is essential for flagellar motor reversals in Shewanella putrefaciens and Vibrio parahaemolyticus
- Authors:
- Brenzinger, Susanne
Pecina, Anna
Mrusek, Devid
Mann, Petra
Völse, Kerstin
Wimmi, Stephan
Ruppert, Ulrike
Becker, Anke
Ringgaard, Simon
Bange, Gert
Thormann, Kai M - Abstract:
- Abstract: The ability of most bacterial flagellar motors to reverse the direction of rotation is crucial for efficient chemotaxis. In Escherichia coli, motor reversals are mediated by binding of phosphorylated chemotaxis protein CheY to components of the flagellar rotor, FliM and FliN, which induces a conformational switch of the flagellar C‐ring. Here, we show that for Shewanella putrefaciens, Vibrio parahaemolyticus and likely a number of other species an additional transmembrane protein, ZomB, is critically required for motor reversals as mutants lacking ZomB exclusively exhibit straightforward swimming also upon full phosphorylation or overproduction of CheY. ZomB is recruited to the cell poles by and is destabilized in the absence of the polar landmark protein HubP. ZomB also co‐localizes to and may thus interact with the flagellar motor. The Δ zomB phenotype was suppressed by mutations in the very C‐terminal region of FliM. We propose that the flagellar motors of Shewanella, Vibrio and numerous other species harboring orthologs to ZomB are locked in counterclockwise rotation and may require interaction with ZomB to enable the conformational switch required for motor reversals. Regulation of ZomB activity or abundance may provide these species with an additional means to modulate chemotaxis efficiency. Abstract : Here, we describe a novel protein, ZomB, which is crucial for the flagellar motors of Shewanella, Vibrio and likely a number of other species to induceAbstract: The ability of most bacterial flagellar motors to reverse the direction of rotation is crucial for efficient chemotaxis. In Escherichia coli, motor reversals are mediated by binding of phosphorylated chemotaxis protein CheY to components of the flagellar rotor, FliM and FliN, which induces a conformational switch of the flagellar C‐ring. Here, we show that for Shewanella putrefaciens, Vibrio parahaemolyticus and likely a number of other species an additional transmembrane protein, ZomB, is critically required for motor reversals as mutants lacking ZomB exclusively exhibit straightforward swimming also upon full phosphorylation or overproduction of CheY. ZomB is recruited to the cell poles by and is destabilized in the absence of the polar landmark protein HubP. ZomB also co‐localizes to and may thus interact with the flagellar motor. The Δ zomB phenotype was suppressed by mutations in the very C‐terminal region of FliM. We propose that the flagellar motors of Shewanella, Vibrio and numerous other species harboring orthologs to ZomB are locked in counterclockwise rotation and may require interaction with ZomB to enable the conformational switch required for motor reversals. Regulation of ZomB activity or abundance may provide these species with an additional means to modulate chemotaxis efficiency. Abstract : Here, we describe a novel protein, ZomB, which is crucial for the flagellar motors of Shewanella, Vibrio and likely a number of other species to induce directional switches of the flagellar rotational direction. Directional switches are required for the cells to change direction of swimming and for chemotaxis. Thus, control of ZomB activity may provide the cells with a means to control the efficiency of navigation during flagella‐mediated swimming. … (more)
- Is Part Of:
- Molecular microbiology. Volume 109:Issue 5(2018)
- Journal:
- Molecular microbiology
- Issue:
- Volume 109:Issue 5(2018)
- Issue Display:
- Volume 109, Issue 5 (2018)
- Year:
- 2018
- Volume:
- 109
- Issue:
- 5
- Issue Sort Value:
- 2018-0109-0005-0000
- Page Start:
- 694
- Page End:
- 709
- Publication Date:
- 2018-08-01
- Subjects:
- Molecular microbiology -- Periodicals
572.829 - Journal URLs:
- http://www.blackwell-synergy.com/servlet/useragent?func=showIssues&code=mmi&close=2003#C2003 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-2958 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/mmi.14070 ↗
- Languages:
- English
- ISSNs:
- 0950-382X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5900.817960
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 14177.xml