Bacterial translation elongation factor EF-Tu interacts and colocalizes with actin-like MreB protein.
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.
Defeu Soufo
Hervé Joël
HJ
Mikrobiologie, Fakultät für Biologie, Universität Freiburg, 79104 Freiburg, Germany. joel.defeusoufo@biologie.uni-freiburg.de
Reimold
Christian
C
Linne
Uwe
U
Knust
Tobias
T
Gescher
Johannes
J
Graumann
Peter L
PL
D001412:Bacillus subtilis / Q000166:cytology* / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D003599:Cytoskeleton / Q000737:chemistry*; D004926:Escherichia coli; D029968:Escherichia coli Proteins / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D010444:Peptide Elongation Factor Tu / Q000378:metabolism*
D003598:Cytoskeletal Proteins; D029968:Escherichia coli Proteins; C078473:MreB protein, E coli; D010444:Peptide Elongation Factor Tu