دورية أكاديمية
Load-dependent adaptation near zero load in the bacterial flagellar motor
| العنوان: | Load-dependent adaptation near zero load in the bacterial flagellar motor |
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| المؤلفون: | Nirody, JA, Nord, AL, Berry, RM |
| بيانات النشر: | Royal Society |
| سنة النشر: | 2020 |
| المجموعة: | Oxford University Research Archive (ORA) |
| الوصف: | The bacterial flagellar motor is an ion-powered transmembrane protein complex which drives swimming in many bacterial species. The motor consists of a cytoplasmic ‘rotor’ ring and a number of ‘stator’ units, which are bound to the cell wall of the bacterium. Recently, it has been shown that the number of functional torque-generating stator units in the motor depends on the external load, and suggested that mechanosensing in the flagellar motor is driven via a ‘catch bond’ mechanism in the motor’s stator units. We present a method that allows us to measure—on a single motor—stator unit dynamics across a large range of external loads, including near the zero-torque limit. By attaching superparamagnetic beads to the flagellar hook, we can control the motor’s speed via a rotating magnetic field. We manipulate the motor to four different speed levels in two different ion-motive force (IMF) conditions. This framework allows for a deeper exploration into the mechanism behind load-dependent remodelling by separating out motor properties, such as rotation speed and energy availability in the form of IMF, that affect the motor torque. The bacterial flagellar motor (BFM) is an ion-driven nanomachine that drives swimming in a variety of bacterial species. The BFM couples the flow of cations (protons, in Escherichia coli) across the bacterial membrane to induce rotation in the flagellum, spinning the filament like a propeller to move the bacterium forward. The flagellar motor generates torque through interactions between the motor’s stator and rotor; specifically, torque is generated via an interaction between a stator unit (in E. coli, comprising the proteins MotA and MotB) and FliG protein ‘spokes’ that line the rotor’s cytoplasmic C-ring (figure 1a). The BFM’s stator can be composed of between 1 and at least 11 independent units. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| العلاقة: | https://ora.ox.ac.uk/objects/uuid:3b9df41c-4e65-4a9e-b448-e7071113e897Test; https://doi.org/10.1098/rsif.2019.0300Test |
| DOI: | 10.1098/rsif.2019.0300 |
| الإتاحة: | https://doi.org/10.1098/rsif.2019.0300Test https://ora.ox.ac.uk/objects/uuid:3b9df41c-4e65-4a9e-b448-e7071113e897Test |
| حقوق: | info:eu-repo/semantics/embargoedAccess |
| رقم الانضمام: | edsbas.14541550 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1098/rsif.2019.0300 |
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