Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Medicine / Faculty of Medicine >
Peer-reviewed Journal Articles, etc >
Folding Latency of Fluorescent Proteins Affects the Mitochondrial Localization of Fusion Proteins
This item is licensed under:Creative Commons Attribution 4.0 International
Title: | Folding Latency of Fluorescent Proteins Affects the Mitochondrial Localization of Fusion Proteins |
Authors: | Kashiwagi, Sayaka Browse this author | Fujioka, Yoichiro Browse this author →KAKEN DB | Satoh, Aya O. Browse this author | Yoshida, Aiko Browse this author →KAKEN DB | Fujioka, Mari Browse this author | Nepal, Prabha Browse this author | Tsuzuki, Atsushi Browse this author | Aoki, Ozora Browse this author | Paudel, Sarad Browse this author →KAKEN DB | Sasajima, Hitoshi Browse this author →KAKEN DB | Ohba, Yusuke Browse this author →KAKEN DB |
Keywords: | fluorescent protein | organelle | fusion protein | mitochondria |
Issue Date: | 2019 |
Publisher: | 一般社団法人 日本細胞生物学会(Japan Society for Cell Biology) |
Journal Title: | Cell structure and function |
Volume: | 44 |
Issue: | 2 |
Start Page: | 183 |
End Page: | 194 |
Publisher DOI: | 10.1247/csf.19028 |
Abstract: | The discovery of fluorescent proteins (FPs) has revolutionized cell biology. The fusion of targeting sequences to FPs enables the investigation of cellular organdies and their dynamics; however, occasionally, such fluorescent fusion proteins (FFPs) exhibit behavior different from that of the native proteins. Here, we constructed a color pallet comprising different organelle markers and found that FFPs targeted to the mitochondria were mislocalized when fused to certain types of FPs. Such FPs included several variants of Aequorea victoria green FP (avGFP) and a monomeric variant of the red FP. Because the FFPs that are mislocalized include FPs with faster maturing or folding mutations, the increase in the maturation rate is likely to prevent their expected localization. Indeed, when we reintroduced amino acid substitutions so that the FP sequences were equivalent to that of mild-type avGFP, FFP localization to the mitochondria was significantly enhanced. Moreover, similar amino acid substitutions improved the localization of mitochondria-targeted pHluorin, which is a pH-sensitive variant of GFP, and its capability to monitor pH changes in the mitochondrial matrix. Our fmdings demonstrate the importance of selecting FPs that maximize FFP function. |
Rights: | https://creativecommons.org/licenses/by/4.0/ |
Type: | article |
URI: | http://hdl.handle.net/2115/76732 |
Appears in Collections: | 医学院・医学研究院 (Graduate School of Medicine / Faculty of Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
|
|