Soufo, Hervé Joël DefeuHervé Joël DefeuSoufoReimold, ChristianChristianReimoldLinne, UweUweLinneKnust, TobiasTobiasKnustGescher, JohannesJohannesGescherGraumann, PeterPeterGraumann2023-02-102023-02-102010-01-28Proceedings of the National Academy of Sciences of the United States of America 107 (7): 3163-3168 (2010-02-16)http://hdl.handle.net/11420/14786We 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.en1091-6490Proceedings of the National Academy of Sciences of the United States of America2010731633168National Acad. of SciencesBacillus subtilisBacterial cytoskeletonCell shapeBiowissenschaften, BiologieBacterial translation elongation factor EF-Tu interacts and colocalizes with actin-like MreB proteinJournal Article10.1073/pnas.091197910720133608Journal Article