2013 Fiscal Year Final Research Report
Elucidation of localization mechanism of the cell surface proteins in bacteria
Project/Area Number |
23580107
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Applied microbiology
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Research Institution | Shinshu University |
Principal Investigator |
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Co-Investigator(Renkei-kenkyūsha) |
ISHIKAWA Shu 奈良先端科学技術大学院大学, バイオサイエンス研究科, 助教 (30359872)
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Project Period (FY) |
2011 – 2013
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Keywords | 細胞表層タンパク質 / 細胞分離酵素 / 細胞壁代謝 / 枯草菌 |
Research Abstract |
DL-endopeptidases are cell wall hydrolases required for shape maintenance and growth in Bacillus subtilis. LytF at septum mainly functions in cell separation. On the other hand, LytE at septum and along sidewall is required for cell elongation in addition to cell separation. In this study, we examined to elucidate what is a key factor required for localization and function of these enzymes. When LytF was expressed with a signal peptide of LytE (SPLytE), it has been localizable not only septum and poles but also along the sidewall. Moreover, SPLytE-LytF could partially suppress a synthetic lethal phenotype of the double mutation in lytE and cwlO. These results strongly suggest that signal peptide governs localization and function of the cell wall hydrolases. Further analyses indicated that the first half region in the hydrophobic part of SPLytE might play an important role for the function of LytE.
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Research Products
(7 results)