Open AccessBacterial translation elongation factor EF-Tu interacts and colocalizes with actin-like MreB protein
Author(s) -
Defeu Soufo Hj,
Christian Reimold,
Uwe Linne,
T Knust,
Johannes Gescher,
Peter L. Graumann
Publication year - 2010
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.0911979107
Subject(s) - mreb , cytoskeleton , actin , microbiology and biotechnology , translation (biology) , elongation factor , bacillus subtilis , biology , cell , rna , genetics , bacteria , ribosome , messenger rna , gene
We show that translation initiation factor EF-Tu plays a second important role in cell shape maintenance in the bacteriumBacillus 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.