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

Kashiwagi, Sayaka; Fujioka, Yoichiro; Satoh, Aya O.; Yoshida, Aiko; Fujioka, Mari; Nepal, Prabha; Tsuzuki, Atsushi; Aoki, Ozora; Paudel, Sarad; Sasajima, Hitoshi; Ohba, Yusuke

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

Kashiwagi, Sayaka; Fujioka, Yoichiro; Satoh, Aya O. et al.

Cell structure and function, 2019, 44(2), 183-194

Permalink : https://hdl.handle.net/2115/76732

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アクセス権	open access
URI	https://hdl.handle.net/2115/76732
タイトル	Folding Latency of Fluorescent Proteins Affects the Mitochondrial Localization of Fusion Proteins
著者	Kashiwagi, Sayaka ; Fujioka, Yoichiro ; Satoh, Aya O. ; Yoshida, Aiko ; Fujioka, Mari ; Nepal, Prabha ; Tsuzuki, Atsushi ; Aoki, Ozora ; Paudel, Sarad ; Sasajima, Hitoshi ; Ohba, Yusuke
著者名 Kashiwagi, Sayaka
e-Rad_Researcher 70597492 著者名 Fujioka, Yoichiro
著者名 Satoh, Aya O.
e-Rad_Researcher 70831288 著者名 Yoshida, Aiko
著者名 Fujioka, Mari
著者名 Nepal, Prabha
著者名 Tsuzuki, Atsushi
著者名 Aoki, Ozora
e-Rad_Researcher 30793939 著者名 Paudel, Sarad
e-Rad_Researcher 00374562 著者名 Sasajima, Hitoshi
e-Rad_Researcher 30333503 著者名 Ohba, Yusuke
言語	英語
キーワード	fluorescent protein
	organelle
	fusion protein
	mitochondria
発行日	2019
出版者	一般社団法人日本細胞生物学会(Japan Society for Cell Biology)
収録物名	Cell structure and function
巻(号)	44(2)
ページ	183-194
抄録	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.
資源タイプ	学術雑誌論文
出版タイプ	Version of Record
権利情報	Creative Commons Attribution 4.0 International
PISSN	0386-7196
関連情報 (isIdenticalTo)	出版社版DOI https://doi.org/10.1247/csf.19028