| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2016: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2015: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2014: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
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| Outline of Final Research Achievements |
A secretory signal sequence located at the N-terminus of a protein directs the protein to the extracellular environment. Signal sequences usually contain an N-terminal basic amino acid followed by a hydrophobic stretch, although no consensus signal sequence has been identified. In this study, mutagenesis and simple modeling of signal sequences was attempted to define optimum signal sequence. Mutagenesis revealed the importance of N-terminal basic residue, length of hydrophobic stretch and Glu following to the stretch in yeast. Hydrophobic stretch region can be substituted with artificial sequence consisting of a repeat of a single hydrophobic amino acid. Stretches consisting of Phe, Leu, Ile, or Met were effective for secretion but the number of residues affected secretory activity. A stretch containing methionine residues showed the highest activity. In human cultured cell, definition of secretion signal is similar but looser compared with the yeast.
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