Mitochondrial targeting sequence of the influenza A virus PB1-F2 protein and its function in mitochondria
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 bo...
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| Veröffentlicht in: | FEBS letters 2004-12, Vol.578 (3), p.331-336 |
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| creator | Yamada, Hiroshi Chounan, Ritsu Higashi, Youichirou Kurihara, Naoki Kido, Hiroshi |
| description | 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. |
| doi_str_mv | 10.1016/j.febslet.2004.11.017 |
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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. 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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. 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Chounan, Ritsu ; Higashi, Youichirou ; Kurihara, Naoki ; Kido, Hiroshi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c525X-54f68d2562d8a4528f3ba138a1ea7d0e189391e1505f82ce6601d68cffa5e42d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies, Monoclonal - metabolism</topic><topic>Arginine - chemistry</topic><topic>Benzimidazoles</topic><topic>Cell Line</topic><topic>Dogs</topic><topic>Fluorescein-5-isothiocyanate</topic><topic>Fluorescent Dyes</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Influenza A virus</topic><topic>Influenza A virus - physiology</topic><topic>Lysine - chemistry</topic><topic>Microscopy, Fluorescence</topic><topic>Mitochondria - metabolism</topic><topic>Mitochondrial membrane potential</topic><topic>Mitochondrion</topic><topic>Mutagenesis, Site-Directed</topic><topic>PB1-F2 protein</topic><topic>Protein Structure, Tertiary</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Sequence Deletion</topic><topic>Targeting sequence</topic><topic>Viral Proteins - chemistry</topic><topic>Viral Proteins - genetics</topic><topic>Viral Proteins - metabolism</topic><topic>Viral Proteins - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yamada, Hiroshi</creatorcontrib><creatorcontrib>Chounan, Ritsu</creatorcontrib><creatorcontrib>Higashi, Youichirou</creatorcontrib><creatorcontrib>Kurihara, Naoki</creatorcontrib><creatorcontrib>Kido, Hiroshi</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yamada, Hiroshi</au><au>Chounan, Ritsu</au><au>Higashi, Youichirou</au><au>Kurihara, Naoki</au><au>Kido, Hiroshi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mitochondrial targeting sequence of the influenza A virus PB1-F2 protein and its function in mitochondria</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2004-12-17</date><risdate>2004</risdate><volume>578</volume><issue>3</issue><spage>331</spage><epage>336</epage><pages>331-336</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><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.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>15589841</pmid><doi>10.1016/j.febslet.2004.11.017</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Wiley Free Content; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Antibodies, Monoclonal - metabolism Arginine - chemistry Benzimidazoles Cell Line Dogs Fluorescein-5-isothiocyanate Fluorescent Dyes HeLa Cells Humans Influenza A virus Influenza A virus - physiology Lysine - chemistry Microscopy, Fluorescence Mitochondria - metabolism Mitochondrial membrane potential Mitochondrion Mutagenesis, Site-Directed PB1-F2 protein Protein Structure, Tertiary Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - metabolism Sequence Deletion Targeting sequence Viral Proteins - chemistry Viral Proteins - genetics Viral Proteins - metabolism Viral Proteins - physiology |
| title | Mitochondrial targeting sequence of the influenza A virus PB1-F2 protein and its function in mitochondria |
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