Partial functional redundancy of MreB isoforms, MreB, Mbl and MreBH, in cell morphogenesis of Bacillus subtilis

Authors

  • Yoshikazu Kawai,

    1. Institute for Cell and Molecular Biosciences, Newcastle University, Medical School, Framlington Place, Newcastle Upon Tyne NE2 4HH, UK.
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  • Kei Asai,

    1. Department of Biochemistry and Molecular Biology, Faculty of Science, Saitama University, 255 Shimo-Ohkubo, Saitama, Saitama 338-8570, Japan.
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  • Jeffery Errington

    Corresponding author
    1. Institute for Cell and Molecular Biosciences, Newcastle University, Medical School, Framlington Place, Newcastle Upon Tyne NE2 4HH, UK.
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*E-mail jeff.errington@newcastle.ac.uk; Tel. (+44) 191 222 8126; Fax (+44) 191 222 7424.

Summary

MreB proteins are bacterial actin homologues thought to have a role in cell shape determination by positioning the cell wall synthetic machinery. Many bacteria, particularly Gram-positives, have more than one MreB isoform. Bacillus subtilis has three, MreB, Mbl and MreBH, which colocalize in a single helical structure. We now show that the helical pattern of peptidoglycan (PG) synthesis in the cylindrical part of the rod-shaped cell is governed by the redundant action of the three MreB isoforms. Single mutants for any one of mreB isoforms can still incorporate PG in a helical pattern and generate a rod shape. However, after depletion of MreB in an mbl mutant (or depletion of all three isoforms) lateral wall PG synthesis was impaired and the cells became spherical and lytic. Overexpression of any one of the MreB isoforms overcame the lethality as well as the defects in lateral PG synthesis and cell shape. Furthermore, MreB and Mbl can associate with the peptidoglycan biosynthetic machinery independently. However, no single MreB isoform was able to support normal growth under various stress conditions, suggesting that the multiple isoforms are used to allow cells to maintain proper growth and morphogenesis under changing and sometimes adverse conditions.

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