期刊
NATURE COMMUNICATIONS
卷 11, 期 1, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-020-15083-5
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资金
- European Research Council [742555]
- Wellcome Trust [201505/Z/16/Z]
- Medical Research Council UK
- European Research Council (ERC) [742555] Funding Source: European Research Council (ERC)
- Wellcome Trust [201505/Z/16/Z] Funding Source: Wellcome Trust
Coordination of outer membrane constriction with septation is critical to faithful division in Gram-negative bacteria and vital to the barrier function of the membrane. This coordination requires the recruitment of the peptidoglycan-binding outer-membrane lipoprotein Pal at division sites by the Tol system. Here, we show that Pal accumulation at Escherichia coli division sites is a consequence of three key functions of the Tol system. First, Tol mobilises Pal molecules in dividing cells, which otherwise diffuse very slowly due to their binding of the cell wall. Second, Tol actively captures mobilised Pal molecules and deposits them at the division septum. Third, the active capture mechanism is analogous to that used by the inner membrane protein TonB to dislodge the plug domains of outer membrane TonB-dependent nutrient transporters. We conclude that outer membrane constriction is coordinated with cell division by active mobilisation-and-capture of Pal at division septa by the Tol system. The lipoprotein Pal participates in the coordination of outer-membrane constriction with septation in Gram-negative bacteria. Here, the authors show that this coordination is mediated by active mobilisation-and-capture of Pal at division septa by the Tol system.
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