2012 Fiscal Year Final Research Report
Molecular mechanism of maintenance of a rod shaped cell in Escherichia coli
| Project/Area Number |
22370067
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Molecular biology
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| Research Institution | National Institute of Genetics |
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Principal Investigator |
NIKI Hironori 国立遺伝学研究所, 系統生物研究センター, 教授 (70208122)
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| Project Period (FY) |
2010 – 2012
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| Keywords | 桿菌 / 球菌 / 細胞壁 / ペプチドグリカン / 細胞骨格 |
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| Research Abstract |
RodZ interacts with MreB and both factors are required to maintain the rod shape of Escherichia coli. The assembly of MreB into filaments regulates the subcellular arrangement of a group of enzymes that synthesizes the peptidoglycan (PG) layer. However, it is still unknown how polymerization of MreB determines the rod shape of bacterial cells. Regulatory factor(s) are likely to be involved in controlling the function and dynamics of MreB. We isolated suppressor mutations to partially recover the rod shape in rodZ deletion mutants and found that some of the suppressor mutations occurred in mreB. All of the mreB mutations were in or in the vicinity of domain IA of MreB. Those mreB mutations changed the property of MreB filaments in vivo. In addition, suppressor mutations were found in the periplasmic regions in PBP2 and RodA, encoded by mrdA and mrdB genes. Similar to MreB and RodZ, PBP2 and RodA are pivotal to the cell wall elongation process. Thus, we found that mutations in domain IA of MreB and in the periplasmic domain of PBP2 and RodA can restore growth and rod shape to ΔrodZ cells, possibly by changing the requirements of MreB in the process.
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[Journal Article] Mutations in cell elongation genes mreB, mrdA and mrdB suppress the shape defect of RodZ-deficient cells2013
Author(s)
Shiomi, D., Toyoda, A., Aizu, T., Ejima,F., Fujiyama, A., Shini, T., Kohara, Y., &Niki, H.
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Journal Title
Mol Microbiol
Volume: 87
Pages: 1029-1044
Peer Reviewed
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[Journal Article] Unbalanced charge distribution as a determinant for dependence of a subset of Escherichia coli membrane proteins on the membrane insertase YidC2011
Author(s)
Gray, A.N., Henderson-Frost, J.M., Boyd, D., Shirafi, S., Niki, H., & Goldberg, M.B
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Journal Title
Peer Reviewed
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[Journal Article] Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds & bundles FtsZ polymers2011
Author(s)
Hale, C.A., Shiomi, D., Liu, B., Bernhardt, T.G., argolin, W., Niki, H., & de Boer, PA
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Journal Title
J Bacteriol
Volume: 193
Pages: 1393-1404
Peer Reviewed
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