The Structure, Composition, and Role of Periplasmic Stator Scaffolds in Polar Bacterial Flagellar Motors
In the bacterial flagellar motor, the cell-wall-anchored stator uses an electrochemical gradient across the cytoplasmic membrane to generate a turning force that is applied to the rotor connected to the flagellar filament. Existing theoretical concepts for the stator function are based on the assump...
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| Format: | Article |
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Frontiers Media S.A.
2021-03-01
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| Series: | Frontiers in Microbiology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fmicb.2021.639490/full |
| _version_ | 1818914813007364096 |
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| author | Xiaotian Zhou Xiaotian Zhou Anna Roujeinikova Anna Roujeinikova Anna Roujeinikova |
| author_facet | Xiaotian Zhou Xiaotian Zhou Anna Roujeinikova Anna Roujeinikova Anna Roujeinikova |
| author_sort | Xiaotian Zhou |
| collection | DOAJ |
| description | In the bacterial flagellar motor, the cell-wall-anchored stator uses an electrochemical gradient across the cytoplasmic membrane to generate a turning force that is applied to the rotor connected to the flagellar filament. Existing theoretical concepts for the stator function are based on the assumption that it anchors around the rotor perimeter by binding to peptidoglycan (P). The existence of another anchoring region on the motor itself has been speculated upon, but is yet to be supported by binding studies. Due to the recent advances in electron cryotomography, evidence has emerged that polar flagellar motors contain substantial proteinaceous periplasmic structures next to the stator, without which the stator does not assemble and the motor does not function. These structures have a morphology of disks, as is the case with Vibrio spp., or a round cage, as is the case with Helicobacter pylori. It is now recognized that such additional periplasmic components are a common feature of polar flagellar motors, which sustain higher torque and greater swimming speeds compared to peritrichous bacteria such as Escherichia coli and Salmonella enterica. This review summarizes the data available on the structure, composition, and role of the periplasmic scaffold in polar bacterial flagellar motors and discusses the new paradigm for how such motors assemble and function. |
| first_indexed | 2024-12-19T23:52:20Z |
| format | Article |
| id | doaj.art-6cea49c658e44a38a98572caa824d0df |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-12-19T23:52:20Z |
| publishDate | 2021-03-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Microbiology |
| spelling | doaj.art-6cea49c658e44a38a98572caa824d0df2022-12-21T20:01:06ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2021-03-011210.3389/fmicb.2021.639490639490The Structure, Composition, and Role of Periplasmic Stator Scaffolds in Polar Bacterial Flagellar MotorsXiaotian Zhou0Xiaotian Zhou1Anna Roujeinikova2Anna Roujeinikova3Anna Roujeinikova4Infection and Immunity Program, Monash Biomedicine Discovery Institute, Monash University, Clayton, VIC, AustraliaDepartment of Microbiology, Monash University, Clayton, VIC, AustraliaInfection and Immunity Program, Monash Biomedicine Discovery Institute, Monash University, Clayton, VIC, AustraliaDepartment of Microbiology, Monash University, Clayton, VIC, AustraliaDepartment of Biochemistry and Molecular Biology, Monash University, Clayton, VIC, AustraliaIn the bacterial flagellar motor, the cell-wall-anchored stator uses an electrochemical gradient across the cytoplasmic membrane to generate a turning force that is applied to the rotor connected to the flagellar filament. Existing theoretical concepts for the stator function are based on the assumption that it anchors around the rotor perimeter by binding to peptidoglycan (P). The existence of another anchoring region on the motor itself has been speculated upon, but is yet to be supported by binding studies. Due to the recent advances in electron cryotomography, evidence has emerged that polar flagellar motors contain substantial proteinaceous periplasmic structures next to the stator, without which the stator does not assemble and the motor does not function. These structures have a morphology of disks, as is the case with Vibrio spp., or a round cage, as is the case with Helicobacter pylori. It is now recognized that such additional periplasmic components are a common feature of polar flagellar motors, which sustain higher torque and greater swimming speeds compared to peritrichous bacteria such as Escherichia coli and Salmonella enterica. This review summarizes the data available on the structure, composition, and role of the periplasmic scaffold in polar bacterial flagellar motors and discusses the new paradigm for how such motors assemble and function.https://www.frontiersin.org/articles/10.3389/fmicb.2021.639490/fullbacterial flagellar motorstructure and functionpolar flagellumtorqueelectron cryotomography |
| spellingShingle | Xiaotian Zhou Xiaotian Zhou Anna Roujeinikova Anna Roujeinikova Anna Roujeinikova The Structure, Composition, and Role of Periplasmic Stator Scaffolds in Polar Bacterial Flagellar Motors Frontiers in Microbiology bacterial flagellar motor structure and function polar flagellum torque electron cryotomography |
| title | The Structure, Composition, and Role of Periplasmic Stator Scaffolds in Polar Bacterial Flagellar Motors |
| title_full | The Structure, Composition, and Role of Periplasmic Stator Scaffolds in Polar Bacterial Flagellar Motors |
| title_fullStr | The Structure, Composition, and Role of Periplasmic Stator Scaffolds in Polar Bacterial Flagellar Motors |
| title_full_unstemmed | The Structure, Composition, and Role of Periplasmic Stator Scaffolds in Polar Bacterial Flagellar Motors |
| title_short | The Structure, Composition, and Role of Periplasmic Stator Scaffolds in Polar Bacterial Flagellar Motors |
| title_sort | structure composition and role of periplasmic stator scaffolds in polar bacterial flagellar motors |
| topic | bacterial flagellar motor structure and function polar flagellum torque electron cryotomography |
| url | https://www.frontiersin.org/articles/10.3389/fmicb.2021.639490/full |
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