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Control of septum thickness by the curvature of SepF polymers.


ABSTRACT: Gram-positive bacteria divide by forming a thick cross wall. How the thickness of this septal wall is controlled is unknown. In this type of bacteria, the key cell division protein FtsZ is anchored to the cell membrane by two proteins, FtsA and/or SepF. We have isolated SepF homologs from different bacterial species and found that they all polymerize into large protein rings with diameters varying from 19 to 44 nm. Interestingly, these values correlated well with the thickness of their septa. To test whether ring diameter determines septal thickness, we tried to construct different SepF chimeras with the purpose to manipulate the diameter of the SepF protein ring. This was indeed possible and confirmed that the conserved core domain of SepF regulates ring diameter. Importantly, when SepF chimeras with different diameters were expressed in the bacterial host Bacillus subtilis, the thickness of its septa changed accordingly. These results strongly support a model in which septal thickness is controlled by curved molecular clamps formed by SepF polymers attached to the leading edge of nascent septa. This also implies that the intrinsic shape of a protein polymer can function as a mold to shape the cell wall.

SUBMITTER: Wenzel M 

PROVIDER: S-EPMC7812789 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature

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Control of septum thickness by the curvature of SepF polymers.

Wenzel Michaela M   Celik Gulsoy Ilkay N IN   Gao Yongqiang Y   Teng Zihao Z   Willemse Joost J   Middelkamp Martijn M   van Rosmalen Mariska G M MGM   Larsen Per W B PWB   van der Wel Nicole N NN   Wuite Gijs J L GJL   Roos Wouter H WH   Hamoen Leendert W LW  

Proceedings of the National Academy of Sciences of the United States of America 20210101 2


Gram-positive bacteria divide by forming a thick cross wall. How the thickness of this septal wall is controlled is unknown. In this type of bacteria, the key cell division protein FtsZ is anchored to the cell membrane by two proteins, FtsA and/or SepF. We have isolated SepF homologs from different bacterial species and found that they all polymerize into large protein rings with diameters varying from 19 to 44 nm. Interestingly, these values correlated well with the thickness of their septa. To  ...[more]

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