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Bacterial translation elongation factor EF-Tu interacts and colocalizes with actin-like MreB protein.


ABSTRACT: We show that translation initiation factor EF-Tu plays a second important role in cell shape maintenance in the bacterium Bacillus subtilis. EF-Tu localizes in a helical pattern underneath the cell membrane and colocalizes with MreB, an actin-like cytoskeletal element setting up rod cell shape. The localization of MreB and of EF-Tu is interdependent, but in contrast to the dynamic MreB filaments, EF-Tu structures are more static and may serve as tracks for MreB filaments. In agreement with this idea, EF-Tu and MreB interact in vivo and in vitro. Lowering of the EF-Tu levels had a minor effect on translation but a strong effect on cell shape and on the localization of MreB, and blocking of the function of EF-Tu in translation did not interfere with the localization of MreB, showing that, directly or indirectly, EF-Tu affects the cytoskeletal MreB structure and thus serves two important functions in a bacterium.

SUBMITTER: Defeu Soufo HJ 

PROVIDER: S-EPMC2840354 | biostudies-literature | 2010 Feb

REPOSITORIES: biostudies-literature

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Bacterial translation elongation factor EF-Tu interacts and colocalizes with actin-like MreB protein.

Defeu Soufo Hervé Joël HJ   Reimold Christian C   Linne Uwe U   Knust Tobias T   Gescher Johannes J   Graumann Peter L PL  

Proceedings of the National Academy of Sciences of the United States of America 20100128 7


We show that translation initiation factor EF-Tu plays a second important role in cell shape maintenance in the bacterium Bacillus subtilis. EF-Tu localizes in a helical pattern underneath the cell membrane and colocalizes with MreB, an actin-like cytoskeletal element setting up rod cell shape. The localization of MreB and of EF-Tu is interdependent, but in contrast to the dynamic MreB filaments, EF-Tu structures are more static and may serve as tracks for MreB filaments. In agreement with this  ...[more]

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