Fueling type III secretion
•The proton motive force (pmf) energizes the rate-limiting step of type III secretion.•The type III secretion system (T3SS) can change the efficiency of pmf utilization to modulate protein export speed.•The ATPase likely renders secreted protein export competent by unfolding them. Type III secretion...
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| Published in | Trends in microbiology (Regular ed.) Vol. 23; no. 5; pp. 296 - 300 |
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| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
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Elsevier Ltd
01.05.2015
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| Abstract | •The proton motive force (pmf) energizes the rate-limiting step of type III secretion.•The type III secretion system (T3SS) can change the efficiency of pmf utilization to modulate protein export speed.•The ATPase likely renders secreted protein export competent by unfolding them.
Type III secretion systems (T3SSs) are complex nanomachines that export proteins from the bacterial cytoplasm across the cell envelope in a single step. They are at the core of the machinery used to assemble the bacterial flagellum, and the needle complex many Gram-negative pathogens use to inject effector proteins into host cells and cause disease. Several models have been put forward to explain how this export is energized, and the mechanism has been the subject of considerable debate. Here we present an overview of these models and discuss their relative merits. Recent evidence suggests that the proton motive force (pmf) is the primary energy source for type III secretion, although contribution from refolding of secreted proteins has not been ruled out. The mechanism by which the pmf is converted to protein export remains enigmatic. |
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| AbstractList | Type III secretion systems are complex nanomachines that export proteins from the bacterial cytoplasm across the cell envelope in a single step. They are at the core of the machinery used to assemble the bacterial flagellum, and the needle complex many Gram-negative pathogens use to inject effector proteins into host cells and cause disease. Several models have been put forward to explain how this export is energized, and the mechanism has been the subject of considerable debate. Here we present an overview of these models and discuss their relative merits. Recent evidence suggests that the proton motive force is the primary energy source for type III secretion, although contribution from refolding of secreted proteins has not been ruled out. The mechanism, by which the proton motive force is converted to protein export, remains enigmatic. Type III secretion systems (T3SSs) are complex nanomachines that export proteins from the bacterial cytoplasm across the cell envelope in a single step. They are at the core of the machinery used to assemble the bacterial flagellum, and the needle complex many Gram-negative pathogens use to inject effector proteins into host cells and cause disease. Several models have been put forward to explain how this export is energized, and the mechanism has been the subject of considerable debate. Here we present an overview of these models and discuss their relative merits. Recent evidence suggests that the proton motive force (pmf) is the primary energy source for type III secretion, although contribution from refolding of secreted proteins has not been ruled out. The mechanism by which the pmf is converted to protein export remains enigmatic.Type III secretion systems (T3SSs) are complex nanomachines that export proteins from the bacterial cytoplasm across the cell envelope in a single step. They are at the core of the machinery used to assemble the bacterial flagellum, and the needle complex many Gram-negative pathogens use to inject effector proteins into host cells and cause disease. Several models have been put forward to explain how this export is energized, and the mechanism has been the subject of considerable debate. Here we present an overview of these models and discuss their relative merits. Recent evidence suggests that the proton motive force (pmf) is the primary energy source for type III secretion, although contribution from refolding of secreted proteins has not been ruled out. The mechanism by which the pmf is converted to protein export remains enigmatic. Type III secretion systems (T3SSs) are complex nanomachines that export proteins from the bacterial cytoplasm across the cell envelope in a single step. They are at the core of the machinery used to assemble the bacterial flagellum, and the needle complex many Gram-negative pathogens use to inject effector proteins into host cells and cause disease. Several models have been put forward to explain how this export is energized, and the mechanism has been the subject of considerable debate. Here we present an overview of these models and discuss their relative merits. Recent evidence suggests that the proton motive force (pmf) is the primary energy source for type III secretion, although contribution from refolding of secreted proteins has not been ruled out. The mechanism by which the pmf is converted to protein export remains enigmatic. •The proton motive force (pmf) energizes the rate-limiting step of type III secretion.•The type III secretion system (T3SS) can change the efficiency of pmf utilization to modulate protein export speed.•The ATPase likely renders secreted protein export competent by unfolding them. Type III secretion systems (T3SSs) are complex nanomachines that export proteins from the bacterial cytoplasm across the cell envelope in a single step. They are at the core of the machinery used to assemble the bacterial flagellum, and the needle complex many Gram-negative pathogens use to inject effector proteins into host cells and cause disease. Several models have been put forward to explain how this export is energized, and the mechanism has been the subject of considerable debate. Here we present an overview of these models and discuss their relative merits. Recent evidence suggests that the proton motive force (pmf) is the primary energy source for type III secretion, although contribution from refolding of secreted proteins has not been ruled out. The mechanism by which the pmf is converted to protein export remains enigmatic. Highlights • The proton motive force (pmf) energizes the rate-limiting step of type III secretion. • The type III secretion system (T3SS) can change the efficiency of pmf utilization to modulate protein export speed. • The ATPase likely renders secreted protein export competent by unfolding them. |
| Author | Rietsch, Arne Lee, Pei-Chung |
| AuthorAffiliation | 1 Cell Biology and Metabolism Program, Eunice Kennedy Shriver National Institute of Child Health and 23 Human Development, National Institutes of Health, Bethesda, MD 20892 2 Dept. of Molecular Biology and Microbiology, Case Western Reserve University, Cleveland, OH, 44106-4960 |
| AuthorAffiliation_xml | – name: 1 Cell Biology and Metabolism Program, Eunice Kennedy Shriver National Institute of Child Health and 23 Human Development, National Institutes of Health, Bethesda, MD 20892 – name: 2 Dept. of Molecular Biology and Microbiology, Case Western Reserve University, Cleveland, OH, 44106-4960 |
| Author_xml | – sequence: 1 givenname: Pei-Chung surname: Lee fullname: Lee, Pei-Chung organization: Cell Biology and Metabolism Program, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA – sequence: 2 givenname: Arne surname: Rietsch fullname: Rietsch, Arne email: arne.rietsch@case.edu organization: Department of Molecular Biology and Microbiology, Case Western Reserve University, Cleveland, OH 44106-4960, USA |
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| Snippet | •The proton motive force (pmf) energizes the rate-limiting step of type III secretion.•The type III secretion system (T3SS) can change the efficiency of pmf... Highlights • The proton motive force (pmf) energizes the rate-limiting step of type III secretion. • The type III secretion system (T3SS) can change the... Type III secretion systems (T3SSs) are complex nanomachines that export proteins from the bacterial cytoplasm across the cell envelope in a single step. They... Type III secretion systems are complex nanomachines that export proteins from the bacterial cytoplasm across the cell envelope in a single step. They are at... |
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| SubjectTerms | Adenosine Triphosphatases - metabolism ATPase Bacteria - metabolism Bacterial Proteins - chemistry Bacterial Proteins - metabolism Cell Membrane - metabolism cytoplasm Cytoplasm - metabolism exports Flagella - metabolism Flagella - physiology Flagella - ultrastructure flagellum Gram-negative bacteria Internal Medicine Models, Biological Models, Molecular Mutation needle complex primary energy protein secretion Protein Transport Protein Unfolding Proton-Motive Force T3SS type III secretion system Type III Secretion Systems - physiology |
| Title | Fueling type III secretion |
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