表題番号：2016B-175
日付：2017/04/10
研究課題 蛍光顕微鏡によるアクチンフィラメントの構造ゆらぎのリアルタイム観察
| 研究者所属（当時） | 資格 | 氏名 | |
|---|---|---|---|
| （代表者） | 理工学術院 先進理工学部 | 教授 | 上田 太郎 |
- 研究成果概要
- Fluorescence intensity of rhodamine (Rh) is affected by its local environment, and the fluorescence intensity of Rh-phalloidin (RhPh) is enhanced by binding to actin filaments. During the initial phase of the binding process of RhPh to actin filaments, fluorescence intensity was non-uniform and punctate along the filaments. Time-lapse observation demonstrated that punctate fluorescence intensity fluctuates over time, and moreover, the fluorescent puncta apparently moved along the filaments. When filaments fully bound with RhPh were partially bleached, the fluorescence was again punctate, and the puncta moved along the filaments. When filaments were labeled by an Alexa dye on the surface of each actin molecule by chemical crosslinking, fluctuation of fluorescence intensity was suppressed. The intensity fluctuations of punctate fluorescence of actin-bound RhPh were also suppressed when filaments were fixed with glutaraldehyde, suggesting that the intensity fluctuations reflect conformational dynamics of actin filaments that affect the local environment of Rh.