Global aggregation analysis of eukaryotic proteins.

2014 Fiscal Year Final Research Report

• Project/Area Number: 25840045
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Biophysics
• Research Institution: Tokyo Institute of Technology
• Principal Investigator: NIWA Tatsuya 東京工業大学, 生命理工学研究科, 助教 (50588530)
• Research Collaborator: TAGUCHI Hideki 東京工業大学, 大学院生命理工学研究科, 教授 (40272710)
• Project Period (FY): 2013-04-01 – 2015-03-31
• Keywords: フォールディング / タンパク質凝集 / 分子シャペロン / 無細胞タンパク質合成系

Outline of Final Research Achievements

To investigate the generality of the results of the comprehensive analysis of protein aggregation in prokaryotic proteins conducted by our groups, we conducted the comprehensive aggregation analysis in eukaryotic proteins in the same way and aimed to uncover the universal nature of the protein aggregation and folding across biological kingdoms.
We investigated the aggregation propensity for ~500 kinds of eukaryotic proteins and analyzed these data, resulting that from the point of view of physicochemical properties, eukaryotic proteins shared the similar tendencies in prokaryotic proteins. However, the specific regions called “intrinsically disordered region”, which are found in almost only eukaryotic proteins, showed the significant relationship with the aggregation propensity of proteins. This result may connect to the understanding of one end of the differences between prokaryotes and eukaryotes from the evolutionary point of view.

Free Research Field

生化学