Development of suramolecular recruiting technology for elucidation of dynamics of protein assemblies involved in cell division

2017 Fiscal Year Final Research Report

• Project/Area Number: 15K12747
• Research Category: Grant-in-Aid for Challenging Exploratory Research
• Allocation Type: Multi-year Fund
• Research Field: Biomolecular chemistry
• Research Institution: Osaka University
• Principal Investigator: Onoda Akira 大阪大学, 工学研究科, 准教授 (60366424)
• Co-Investigator(Renkei-kenkyūsha): HAYASHI Takashi 大阪大学, 大学院工学研究科, 教授 (20222226)
• Project Period (FY): 2015-04-01 – 2018-03-31
• Keywords: 細胞分裂 / タンパク質集合体 / 超分子相互作用

Outline of Final Research Achievements

Cell division protein FtsZ assembles as a filamentous structure at midcell leading to the formation of a ring-shaped structure (Z-ring) which constricts to initiate cytoplasmic division. The event involves the conformational change of FtsZ assembly triggered by GTP hydrolysis. To unravel the dynamics and functional aspects of FtsZ assembly, a system in which the assembled structure of engineered FtsZ is perturbed by a supramolecular interaction with external adaptor proteins was developed. FtsZ protein fused with a Strep-tag and a membrane-targeting peptide (Strep-FtsZ-mtp) was found to form a filamentous structure similar to that of the native protein. AFM measurements visualized that the assembly of Strep-FtsZ-mtp was enforced to form a curved structure by the interaction between Strep-tag and streptavidin (Sav). The assembly embedded in a liposome was imaged by fluorescence microscopy.

Free Research Field

バイオ関連化学