2013 Fiscal Year Final Research Report
Systematic discovery of N-end-rule substrate proteins
Project/Area Number |
22685017
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Research Category |
Grant-in-Aid for Young Scientists (A)
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Allocation Type | Single-year Grants |
Research Field |
Chemistry related to living body
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Research Institution | The University of Electro-Communications (2011-2013) Okayama University (2010) |
Principal Investigator |
TAKI Masumi 電気通信大学, 情報理工学(系)研究科, 准教授 (70362952)
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Project Period (FY) |
2010-04-01 – 2014-03-31
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Keywords | N末端ルール / NEXT-A反応 / L/F-転移酵素 / 不安定化蛋白質 |
Research Abstract |
i) A mutant yeast strain that defects protein degradation system (i.e. ubiquitin ligase) survives when a destabilizing protein is accumulated inside the cell. At that time, the cell overexpresses Obr1 protein to overcome the stressed condition. ii) Kinetic analysis of L/F-transferase with N-end-rule substrate peptides posessing different N-terminal penultimate residues is systematically performed. This analysis suggests that the side chain of the residue affects substrate-binding afffinity towards the transferase. It gives biological insight into the effect of the penultimate amino acid on substrate specificity of natural proteins to be degraded via the N-end rule pathway.
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