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

Proc Natl Acad Sci U S A. 2010 Feb 16;107(7):3163-8. doi: 10.1073/pnas.0911979107. Epub 2010 Jan 28.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus subtilis / cytology*
  • Bacillus subtilis / metabolism
  • Cytoskeletal Proteins / metabolism*
  • Cytoskeleton / chemistry*
  • Escherichia coli
  • Escherichia coli Proteins / metabolism*
  • Microscopy, Fluorescence
  • Peptide Elongation Factor Tu / metabolism*


  • Cytoskeletal Proteins
  • Escherichia coli Proteins
  • MreB protein, E coli
  • Peptide Elongation Factor Tu