Search for important sites in protein structure formation and elucidation of selection factors in their evolution

2019 Fiscal Year Final Research Report

• Project/Area Number: 17K07368
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Biophysics
• Research Institution: Kyoto Prefectural University
• Principal Investigator: Takano Kazufumi 京都府立大学, 生命環境科学研究科, 教授 (40346185)
• Project Period (FY): 2017-04-01 – 2020-03-31
• Keywords: タンパク質

Outline of Final Research Achievements

In this work, in order to get broader knowledge on the relationship between amino acid substitutions and protein function/structure, we attempted to extract ‘mutable and fatal sites’ by ‘random mutation’ using ‘stable hyperthermophilic proteins’. The proteins applied were an esterase from Sulfolobus tokodaii (Sto-Est) and a subtilisin from Thermococcus kodakarensis (Tk-Sub). These proteins have been well studied for their function, structure and stability, and have also been used in random mutation experiments; we have extensive published and unpublished data on the activity and sequence for random mutations of these proteins. This study has revealed a portion of the properties at conserved sites that can be mutated and non-conserved sites that are not suitable for mutation.

Free Research Field

生物物理

Academic Significance and Societal Importance of the Research Achievements

今日、タンパク質の構造構築メカニズムに関して、計算機を用いた研究が増加してきているが、実験を通して得られる知見もまだまだ多くある。特に本研究のような網羅的解析が有効である。本研究は、研究代表者がこれまで行ってきた個々のタンパク質の安定性・フォールディング研究から構造構築網羅的解析、物性と進化の関係も含んだ新たな研究を展開するものである。