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Folding Latency of Fluorescent Proteins Affects the Mitochondrial Localization of Fusion Proteins

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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)

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