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        <identifier>oai:repository.dl.itc.u-tokyo.ac.jp:00003730</identifier>
        <datestamp>2022-12-19T03:45:22Z</datestamp>
        <setSpec>110:244:245</setSpec>
        <setSpec>9:233:234</setSpec>
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          <dc:title>原子間力顕微鏡を用いたセンサータンパクMsb2pとHkr1pの機械的性質測定系の構築</dc:title>
          <dc:title>Construction of Mechanical Property Measurement System of Sensor Protein Msb2p and Hkr1p Using Atomic Force Microscopy</dc:title>
          <dc:creator>Hiramoto, Ryusuke</dc:creator>
          <dc:creator>8781</dc:creator>
          <dc:subject>464</dc:subject>
          <dc:subject>出芽酵母</dc:subject>
          <dc:subject>原子間力顕微鏡</dc:subject>
          <dc:subject>センサータンパク質</dc:subject>
          <dc:description>修士(生命科学)</dc:description>
          <dc:description>In the yeast Saccharomyces cerevisiae, remodeling of cellular function is required for the response to extracellular stresses. This response is initiated when a sensor protein spanning the plasma membrane perceives stresses. However, its sensing mechanism towards variety of stresses is obscure. To obtain the details on the mechanism and function of a sensor protein, Dufrêne and his co-workers established a method to evaluate the mechanical properties of sensor proteins using the atomic force microscopy (AFM), and clarified that Wsc1p, a sensor protein of cell wall integrity pathway, behaves like a Hookean nanospring. It is possible that the Wsc1p perceives the tension of the glucan chain caused by stresses such as hypo-osmotic shock. The study further revealed that glycosylated Wsc1p perceives the mechanical tension enforced on the cell wall through its linkage with the glucan chain of the call wall. In hyperosmotic condition, cell wall is also subjected to change in its tension due to the rapid shift in turgor pressure. Thus, sensing mechanism of hyperosmotic environment is likely to have a similar property to Wsc1p, however, the difference and similarity of their sensing mechanisms were never investigated. Here I focused on Msb2p and Hkr1p, putative sensor proteins of high osmolarity glycerol (HOG) pathway which is activated by hyperosmotic shock, to clarify the nature of the sensor proteins and its sensing mechanism. In this study, I prepared the construct suitable for AFM analysis. The modified Msb2p was confirmed its function and existence in mother cell surface. The construction and confirmation of the fusion protein is essential for the further study using AFM.</dc:description>
          <dc:description>thesis</dc:description>
          <dc:date>2011-03-24</dc:date>
          <dc:date>2011-03-24</dc:date>
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          <dc:format>application/pdf</dc:format>
          <dc:identifier>https://repository.dl.itc.u-tokyo.ac.jp/record/3730/files/K-02679.pdf</dc:identifier>
          <dc:identifier>https://repository.dl.itc.u-tokyo.ac.jp/record/3730/files/K-02679-a.pdf</dc:identifier>
          <dc:identifier>http://hdl.handle.net/2261/48927</dc:identifier>
          <dc:identifier>https://repository.dl.itc.u-tokyo.ac.jp/records/3730</dc:identifier>
          <dc:language>eng</dc:language>
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