Dynamic localization and interaction with other Bacillus subtilis actin-like proteins are important for the function of MreB
Autor: | Peter L. Graumann, Hervé Joël Defeu Soufo |
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Rok vydání: | 2006 |
Předmět: |
Genetics
Escherichia coli Proteins Mutant Membrane Proteins Bacillus subtilis Biology biology.organism_classification Cell morphology Microbiology MreB Actins Cell biology Chromosome segregation Cell membrane medicine.anatomical_structure Bacterial Proteins Membrane protein Genes Bacterial Morphogenesis medicine Molecular Biology Actin |
Zdroj: | Molecular Microbiology. 62:1340-1356 |
ISSN: | 1365-2958 0950-382X |
DOI: | 10.1111/j.1365-2958.2006.05457.x |
Popis: | Bacterial actin-like proteins play a key role in cell morphology and in chromosome segregation. Many bacteria, like Bacillus subtilis, contain three genes encoding actin-like proteins, called mreB, mbl and mreBH in B. subtilis. We show that MreB and Mbl colocalize extensively within live cells, and that all three B. subtilis actin paralogues interact with each other underneath the cell membrane. A mutation in the phosphate 2 motif of MreB had a dominant negative effect on cell morphology and on chromosome segregation. Expression of this mutant allele of MreB interfered with the dynamic localization of Mbl. These experiments show that the interaction between MreB and Mbl has physiological significance. An mreB deletion strain can grow under special media conditions, however, depletion of Mbl in this mutant background abolished growth, indicating that actin paralogues can partially complement each other. The membrane protein MreC was found to interact with Mbl, but not with MreB, revealing a clear distinction between the function of the two paralogues. The phosphate 2 mutant MreB protein allowed for filament formation of mutant or wild-type MreB, but abolished the dynamic reorganization of the filaments. The latter mutation led to a strong reduction, but not complete loss, of function of MreB, both in terms of chromosome segregation and of cell morphology. Our work shows that that the dynamic localization of MreB is essential for the proper activity of the actin-like protein and that the interactions between MreB paralogues have important physiological significance. |
Databáze: | OpenAIRE |
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