Distinct Domains Control the Addressing and the Insertion of Bax into Mitochondria
The translocation of Bax from the cytosol into the mitochondrial outer membrane is a central event during apoptosis. We report that beyond the addressing step, which involves its first α-helix (hα1), the helices α5 and α6 (hα5α6) are responsible for the insertion of Bax into mitochondrial outer memb...
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| Veröffentlicht in: | The Journal of biological chemistry 2005-03, Vol.280 (11), p.10587-10598 |
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| creator | Cartron, Pierre-François Arokium, Hubert Oliver, Lisa Meflah, Khaled Manon, Stephen Vallette, François M. |
| description | The translocation of Bax from the cytosol into the mitochondrial outer membrane is a central event during apoptosis. We report that beyond the addressing step, which involves its first α-helix (hα1), the helices α5 and α6 (hα5α6) are responsible for the insertion of Bax into mitochondrial outer membrane bilayer. The translocation of Bax to mitochondria is associated with specific changes in the conformation of the protein that are under the control of two prolines: Pro-13, which controls the unfolding of hα1, and Pro-168, a proline located immediately before the hydrophobic carboxyl-terminal end (i.e. helix α9, hα9), which controls the disclosure of hα5α6. An additional step, the disruption of an electrostatic bond formed between Asp-33 (hα1) and Lys-64 (BH3), allows the mitochondria addressing of Bax. We conclude that, although the intramolecular interactions of hα1 with the BH3 region control the addressing of Bax to mitochondria, the Pro-168 is involved in the control of its membrane insertion through hα5α6. |
| doi_str_mv | 10.1074/jbc.M409714200 |
| format | Article |
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We report that beyond the addressing step, which involves its first α-helix (hα1), the helices α5 and α6 (hα5α6) are responsible for the insertion of Bax into mitochondrial outer membrane bilayer. The translocation of Bax to mitochondria is associated with specific changes in the conformation of the protein that are under the control of two prolines: Pro-13, which controls the unfolding of hα1, and Pro-168, a proline located immediately before the hydrophobic carboxyl-terminal end (i.e. helix α9, hα9), which controls the disclosure of hα5α6. An additional step, the disruption of an electrostatic bond formed between Asp-33 (hα1) and Lys-64 (BH3), allows the mitochondria addressing of Bax. We conclude that, although the intramolecular interactions of hα1 with the BH3 region control the addressing of Bax to mitochondria, the Pro-168 is involved in the control of its membrane insertion through hα5α6.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M409714200</identifier><identifier>PMID: 15590655</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Apoptosis ; Aspartic Acid - chemistry ; Base Sequence ; bcl-2-Associated X Protein ; Cell-Free System ; Cytosol - metabolism ; Electrophoresis, Polyacrylamide Gel ; Immunoprecipitation ; Lipid Bilayers ; Liver - metabolism ; Lysine - chemistry ; Microscopy, Confocal ; Mitochondria - metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; Plasmids - metabolism ; Proline - chemistry ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Transport ; Proto-Oncogene Proteins c-bcl-2 - chemistry ; Proto-Oncogene Proteins c-bcl-2 - metabolism ; Rats ; Static Electricity ; Subcellular Fractions - metabolism ; Transfection ; Transgenes ; Two-Hybrid System Techniques</subject><ispartof>The Journal of biological chemistry, 2005-03, Vol.280 (11), p.10587-10598</ispartof><rights>2005 © 2005 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c411t-6591ba4b1046724e2cb0ab71fd9ff51e1851527bc83f85686ca56e26e95a5fb33</citedby><cites>FETCH-LOGICAL-c411t-6591ba4b1046724e2cb0ab71fd9ff51e1851527bc83f85686ca56e26e95a5fb33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15590655$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cartron, Pierre-François</creatorcontrib><creatorcontrib>Arokium, Hubert</creatorcontrib><creatorcontrib>Oliver, Lisa</creatorcontrib><creatorcontrib>Meflah, Khaled</creatorcontrib><creatorcontrib>Manon, Stephen</creatorcontrib><creatorcontrib>Vallette, François M.</creatorcontrib><title>Distinct Domains Control the Addressing and the Insertion of Bax into Mitochondria</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The translocation of Bax from the cytosol into the mitochondrial outer membrane is a central event during apoptosis. We report that beyond the addressing step, which involves its first α-helix (hα1), the helices α5 and α6 (hα5α6) are responsible for the insertion of Bax into mitochondrial outer membrane bilayer. The translocation of Bax to mitochondria is associated with specific changes in the conformation of the protein that are under the control of two prolines: Pro-13, which controls the unfolding of hα1, and Pro-168, a proline located immediately before the hydrophobic carboxyl-terminal end (i.e. helix α9, hα9), which controls the disclosure of hα5α6. An additional step, the disruption of an electrostatic bond formed between Asp-33 (hα1) and Lys-64 (BH3), allows the mitochondria addressing of Bax. We conclude that, although the intramolecular interactions of hα1 with the BH3 region control the addressing of Bax to mitochondria, the Pro-168 is involved in the control of its membrane insertion through hα5α6.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Aspartic Acid - chemistry</subject><subject>Base Sequence</subject><subject>bcl-2-Associated X Protein</subject><subject>Cell-Free System</subject><subject>Cytosol - metabolism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Immunoprecipitation</subject><subject>Lipid Bilayers</subject><subject>Liver - metabolism</subject><subject>Lysine - chemistry</subject><subject>Microscopy, Confocal</subject><subject>Mitochondria - metabolism</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Mutation</subject><subject>Plasmids - metabolism</subject><subject>Proline - chemistry</subject><subject>Protein Conformation</subject><subject>Protein Folding</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Transport</subject><subject>Proto-Oncogene Proteins c-bcl-2 - chemistry</subject><subject>Proto-Oncogene Proteins c-bcl-2 - metabolism</subject><subject>Rats</subject><subject>Static Electricity</subject><subject>Subcellular Fractions - metabolism</subject><subject>Transfection</subject><subject>Transgenes</subject><subject>Two-Hybrid System Techniques</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kM1LAzEQxYMotlavHiUHr1szu5vd7LG2fhRaBFHwFpJstk1pk5LEr__eaAs9OZeB4fce8x5Cl0CGQOryZiXVcF6SpoYyJ-QI9YGwIisovB2jPiE5ZE1OWQ-dhbAiacoGTlEPKG1IRWkfPU9MiMaqiCduI4wNeOxs9G6N41LjUdt6HYKxCyxs-3ea2qB9NM5i1-Fb8YWNjQ7PTXRq6WzrjThHJ51YB32x3wP0en_3Mn7MZk8P0_FolqkSIGYVbUCKUgIpqzovda4kEbKGrm26joIGRoHmtVSs6BitWKUErXRe6YYK2smiGKDhzld5F4LXHd96sxH-mwPhv-XwVA4_lJMEVzvB9l1udHvA920k4HoHLM1i-Wm85tKkWHrDc5YsIblSVieM7TCd0n0Y7XlQRlul2yRRkbfO_PfCD1n1fl0</recordid><startdate>20050318</startdate><enddate>20050318</enddate><creator>Cartron, Pierre-François</creator><creator>Arokium, Hubert</creator><creator>Oliver, Lisa</creator><creator>Meflah, Khaled</creator><creator>Manon, Stephen</creator><creator>Vallette, François M.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20050318</creationdate><title>Distinct Domains Control the Addressing and the Insertion of Bax into Mitochondria</title><author>Cartron, Pierre-François ; Arokium, Hubert ; Oliver, Lisa ; Meflah, Khaled ; Manon, Stephen ; Vallette, François M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c411t-6591ba4b1046724e2cb0ab71fd9ff51e1851527bc83f85686ca56e26e95a5fb33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Aspartic Acid - chemistry</topic><topic>Base Sequence</topic><topic>bcl-2-Associated X Protein</topic><topic>Cell-Free System</topic><topic>Cytosol - metabolism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Immunoprecipitation</topic><topic>Lipid Bilayers</topic><topic>Liver - metabolism</topic><topic>Lysine - chemistry</topic><topic>Microscopy, Confocal</topic><topic>Mitochondria - metabolism</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Mutation</topic><topic>Plasmids - metabolism</topic><topic>Proline - chemistry</topic><topic>Protein Conformation</topic><topic>Protein Folding</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>Protein Transport</topic><topic>Proto-Oncogene Proteins c-bcl-2 - chemistry</topic><topic>Proto-Oncogene Proteins c-bcl-2 - metabolism</topic><topic>Rats</topic><topic>Static Electricity</topic><topic>Subcellular Fractions - metabolism</topic><topic>Transfection</topic><topic>Transgenes</topic><topic>Two-Hybrid System Techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cartron, Pierre-François</creatorcontrib><creatorcontrib>Arokium, Hubert</creatorcontrib><creatorcontrib>Oliver, Lisa</creatorcontrib><creatorcontrib>Meflah, Khaled</creatorcontrib><creatorcontrib>Manon, Stephen</creatorcontrib><creatorcontrib>Vallette, François M.</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><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cartron, Pierre-François</au><au>Arokium, Hubert</au><au>Oliver, Lisa</au><au>Meflah, Khaled</au><au>Manon, Stephen</au><au>Vallette, François M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Distinct Domains Control the Addressing and the Insertion of Bax into Mitochondria</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2005-03-18</date><risdate>2005</risdate><volume>280</volume><issue>11</issue><spage>10587</spage><epage>10598</epage><pages>10587-10598</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The translocation of Bax from the cytosol into the mitochondrial outer membrane is a central event during apoptosis. We report that beyond the addressing step, which involves its first α-helix (hα1), the helices α5 and α6 (hα5α6) are responsible for the insertion of Bax into mitochondrial outer membrane bilayer. The translocation of Bax to mitochondria is associated with specific changes in the conformation of the protein that are under the control of two prolines: Pro-13, which controls the unfolding of hα1, and Pro-168, a proline located immediately before the hydrophobic carboxyl-terminal end (i.e. helix α9, hα9), which controls the disclosure of hα5α6. An additional step, the disruption of an electrostatic bond formed between Asp-33 (hα1) and Lys-64 (BH3), allows the mitochondria addressing of Bax. We conclude that, although the intramolecular interactions of hα1 with the BH3 region control the addressing of Bax to mitochondria, the Pro-168 is involved in the control of its membrane insertion through hα5α6.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15590655</pmid><doi>10.1074/jbc.M409714200</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Animals Apoptosis Aspartic Acid - chemistry Base Sequence bcl-2-Associated X Protein Cell-Free System Cytosol - metabolism Electrophoresis, Polyacrylamide Gel Immunoprecipitation Lipid Bilayers Liver - metabolism Lysine - chemistry Microscopy, Confocal Mitochondria - metabolism Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Mutation Plasmids - metabolism Proline - chemistry Protein Conformation Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Protein Transport Proto-Oncogene Proteins c-bcl-2 - chemistry Proto-Oncogene Proteins c-bcl-2 - metabolism Rats Static Electricity Subcellular Fractions - metabolism Transfection Transgenes Two-Hybrid System Techniques |
| title | Distinct Domains Control the Addressing and the Insertion of Bax into Mitochondria |
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