Mitochondrial targeting sequence of the influenza A virus PB1-F2 protein and its function in mitochondria

Hiroshi Yamada; Ritsu Chounan; Youichirou Higashi; Naoki Kurihara; Hiroshi Kido

doi:10.1016/j.febslet.2004.11.017

Mitochondrial targeting sequence of the influenza A virus PB1-F2 protein and its function in mitochondria

Hiroshi Yamada, Ritsu Chounan, Youichirou Higashi, Naoki Kurihara, Hiroshi Kido

微生物学講座

研究成果: ジャーナルへの寄稿 › 学術論文 › 査読

117 被引用数 (Scopus)

抄録

The influenza A virus PB1-F2 protein predominantly localizes in the mitochondria of virus-infected cells. A series of cDNAs encoding N- and C-terminal deletion mutants and site-directed mutagenesis of the basic residues of PB1-F2 appended to 3xFLAG revealed the domain from residues 46 to 75 to be both necessary and sufficient for mitochondrial targeting. In addition, the subdomain residues 63-75 and both Lys73 and Arg75 are minimally required for mitochondrial localization. Transfection of untagged- and 3xFLAG tagged-PB1-F2 into Vero, HeLa and MDCK cells changed the mitochondrial morphology from a filamentous to a dotted structure and suppressed the inner-membrane potential.

本文言語	英語
ページ（範囲）	331-336
ページ数	6
ジャーナル	FEBS Letters
巻	578
号	3
DOI	https://doi.org/10.1016/j.febslet.2004.11.017
出版ステータス	出版済み - 2004/12/17

ASJC Scopus 主題領域

生物理学
構造生物学
生化学
分子生物学
遺伝学
細胞生物学

文献へのアクセス

10.1016/j.febslet.2004.11.017

引用スタイル

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title = "Mitochondrial targeting sequence of the influenza A virus PB1-F2 protein and its function in mitochondria",

abstract = "The influenza A virus PB1-F2 protein predominantly localizes in the mitochondria of virus-infected cells. A series of cDNAs encoding N- and C-terminal deletion mutants and site-directed mutagenesis of the basic residues of PB1-F2 appended to 3xFLAG revealed the domain from residues 46 to 75 to be both necessary and sufficient for mitochondrial targeting. In addition, the subdomain residues 63-75 and both Lys73 and Arg75 are minimally required for mitochondrial localization. Transfection of untagged- and 3xFLAG tagged-PB1-F2 into Vero, HeLa and MDCK cells changed the mitochondrial morphology from a filamentous to a dotted structure and suppressed the inner-membrane potential.",

keywords = "Influenza A virus, Mitochondrial membrane potential, Mitochondrion, PB1-F2 protein, Targeting sequence",

author = "Hiroshi Yamada and Ritsu Chounan and Youichirou Higashi and Naoki Kurihara and Hiroshi Kido",

note = "Funding Information: This study was supported in part by grants from the Cluster project and Grants-in-Aid (13557014 and 16790580) of Japanese Ministry of Education, Culture, Sports, Science and Technology. We appreciate review of the manuscript prior to submission by Pacific Edit.",

year = "2004",

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doi = "10.1016/j.febslet.2004.11.017",

language = "英語",

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T1 - Mitochondrial targeting sequence of the influenza A virus PB1-F2 protein and its function in mitochondria

AU - Yamada, Hiroshi

AU - Chounan, Ritsu

AU - Higashi, Youichirou

AU - Kurihara, Naoki

AU - Kido, Hiroshi

N1 - Funding Information: This study was supported in part by grants from the Cluster project and Grants-in-Aid (13557014 and 16790580) of Japanese Ministry of Education, Culture, Sports, Science and Technology. We appreciate review of the manuscript prior to submission by Pacific Edit.

PY - 2004/12/17

Y1 - 2004/12/17

N2 - The influenza A virus PB1-F2 protein predominantly localizes in the mitochondria of virus-infected cells. A series of cDNAs encoding N- and C-terminal deletion mutants and site-directed mutagenesis of the basic residues of PB1-F2 appended to 3xFLAG revealed the domain from residues 46 to 75 to be both necessary and sufficient for mitochondrial targeting. In addition, the subdomain residues 63-75 and both Lys73 and Arg75 are minimally required for mitochondrial localization. Transfection of untagged- and 3xFLAG tagged-PB1-F2 into Vero, HeLa and MDCK cells changed the mitochondrial morphology from a filamentous to a dotted structure and suppressed the inner-membrane potential.

AB - The influenza A virus PB1-F2 protein predominantly localizes in the mitochondria of virus-infected cells. A series of cDNAs encoding N- and C-terminal deletion mutants and site-directed mutagenesis of the basic residues of PB1-F2 appended to 3xFLAG revealed the domain from residues 46 to 75 to be both necessary and sufficient for mitochondrial targeting. In addition, the subdomain residues 63-75 and both Lys73 and Arg75 are minimally required for mitochondrial localization. Transfection of untagged- and 3xFLAG tagged-PB1-F2 into Vero, HeLa and MDCK cells changed the mitochondrial morphology from a filamentous to a dotted structure and suppressed the inner-membrane potential.

KW - Influenza A virus

KW - Mitochondrial membrane potential

KW - Mitochondrion

KW - PB1-F2 protein

KW - Targeting sequence

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U2 - 10.1016/j.febslet.2004.11.017

DO - 10.1016/j.febslet.2004.11.017

M3 - 学術論文

C2 - 15589841

AN - SCOPUS:10044257654

SN - 0014-5793

VL - 578

SP - 331

EP - 336

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

Mitochondrial targeting sequence of the influenza A virus PB1-F2 protein and its function in mitochondria

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