Polar Residues and Their Positional Context Dictate the Transmembrane Domain Interactions of Influenza A Neuraminidases*
Identifieur interne : 000878 ( Ncbi/Merge ); précédent : 000877; suivant : 000879Polar Residues and Their Positional Context Dictate the Transmembrane Domain Interactions of Influenza A Neuraminidases*
Auteurs : Johan Nordholm [Suède] ; Diogo V. Da Silva [Suède] ; Justina Damjanovic [Suède] ; Dan Dou [Suède] ; Robert Daniels [Suède]Source :
- The Journal of Biological Chemistry [ 0021-9258 ] ; 2013.
Abstract
Url:
DOI: 10.1074/jbc.M112.440230
PubMed: 23447533
PubMed Central: 3624445
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Polar Residues and Their Positional Context Dictate the Transmembrane Domain Interactions of Influenza A Neuraminidases<xref ref-type="fn" rid="FN1">*</xref></title><author><name sortKey="Nordholm, Johan" sort="Nordholm, Johan" uniqKey="Nordholm J" first="Johan" last="Nordholm">Johan Nordholm</name><affiliation wicri:level="4"><nlm:aff id="aff1">From the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden</nlm:aff><country xml:lang="fr">Suède</country><wicri:regionArea>From the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm</wicri:regionArea><orgName type="university">Université de Stockholm</orgName><placeName><settlement type="city">Stockholm</settlement><region nuts="1">Svealand</region><region nuts="1">Comté de Stockholm</region></placeName></affiliation></author><author><name sortKey="Da Silva, Diogo V" sort="Da Silva, Diogo V" uniqKey="Da Silva D" first="Diogo V." last="Da Silva">Diogo V. Da Silva</name><affiliation wicri:level="4"><nlm:aff id="aff1">From the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden</nlm:aff><country xml:lang="fr">Suède</country><wicri:regionArea>From the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm</wicri:regionArea><orgName type="university">Université de Stockholm</orgName><placeName><settlement type="city">Stockholm</settlement><region nuts="1">Svealand</region><region nuts="1">Comté de Stockholm</region></placeName></affiliation></author><author><name sortKey="Damjanovic, Justina" sort="Damjanovic, Justina" uniqKey="Damjanovic J" first="Justina" last="Damjanovic">Justina Damjanovic</name><affiliation wicri:level="4"><nlm:aff id="aff1">From the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden</nlm:aff><country xml:lang="fr">Suède</country><wicri:regionArea>From the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm</wicri:regionArea><orgName type="university">Université de Stockholm</orgName><placeName><settlement type="city">Stockholm</settlement><region nuts="1">Svealand</region><region nuts="1">Comté de Stockholm</region></placeName></affiliation></author><author><name sortKey="Dou, Dan" sort="Dou, Dan" uniqKey="Dou D" first="Dan" last="Dou">Dan Dou</name><affiliation wicri:level="4"><nlm:aff id="aff1">From the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden</nlm:aff><country xml:lang="fr">Suède</country><wicri:regionArea>From the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm</wicri:regionArea><orgName type="university">Université de Stockholm</orgName><placeName><settlement type="city">Stockholm</settlement><region nuts="1">Svealand</region><region nuts="1">Comté de Stockholm</region></placeName></affiliation></author><author><name sortKey="Daniels, Robert" sort="Daniels, Robert" uniqKey="Daniels R" first="Robert" last="Daniels">Robert Daniels</name><affiliation wicri:level="4"><nlm:aff id="aff1">From the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden</nlm:aff><country xml:lang="fr">Suède</country><wicri:regionArea>From the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm</wicri:regionArea><orgName type="university">Université de Stockholm</orgName><placeName><settlement type="city">Stockholm</settlement><region nuts="1">Svealand</region><region nuts="1">Comté de Stockholm</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">23447533</idno><idno type="pmc">3624445</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3624445</idno><idno type="RBID">PMC:3624445</idno><idno type="doi">10.1074/jbc.M112.440230</idno><date when="2013">2013</date><idno type="wicri:Area/Pmc/Corpus">000622</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000622</idno><idno type="wicri:Area/Pmc/Curation">000622</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000622</idno><idno type="wicri:Area/Pmc/Checkpoint">000588</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000588</idno><idno type="wicri:Area/Ncbi/Merge">000878</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Polar Residues and Their Positional Context Dictate the Transmembrane Domain Interactions of Influenza A Neuraminidases<xref ref-type="fn" rid="FN1">*</xref></title><author><name sortKey="Nordholm, Johan" sort="Nordholm, Johan" uniqKey="Nordholm J" first="Johan" last="Nordholm">Johan Nordholm</name><affiliation wicri:level="4"><nlm:aff id="aff1">From the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden</nlm:aff><country xml:lang="fr">Suède</country><wicri:regionArea>From the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm</wicri:regionArea><orgName type="university">Université de Stockholm</orgName><placeName><settlement type="city">Stockholm</settlement><region nuts="1">Svealand</region><region nuts="1">Comté de Stockholm</region></placeName></affiliation></author><author><name sortKey="Da Silva, Diogo V" sort="Da Silva, Diogo V" uniqKey="Da Silva D" first="Diogo V." last="Da Silva">Diogo V. Da Silva</name><affiliation wicri:level="4"><nlm:aff id="aff1">From the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden</nlm:aff><country xml:lang="fr">Suède</country><wicri:regionArea>From the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm</wicri:regionArea><orgName type="university">Université de Stockholm</orgName><placeName><settlement type="city">Stockholm</settlement><region nuts="1">Svealand</region><region nuts="1">Comté de Stockholm</region></placeName></affiliation></author><author><name sortKey="Damjanovic, Justina" sort="Damjanovic, Justina" uniqKey="Damjanovic J" first="Justina" last="Damjanovic">Justina Damjanovic</name><affiliation wicri:level="4"><nlm:aff id="aff1">From the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden</nlm:aff><country xml:lang="fr">Suède</country><wicri:regionArea>From the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm</wicri:regionArea><orgName type="university">Université de Stockholm</orgName><placeName><settlement type="city">Stockholm</settlement><region nuts="1">Svealand</region><region nuts="1">Comté de Stockholm</region></placeName></affiliation></author><author><name sortKey="Dou, Dan" sort="Dou, Dan" uniqKey="Dou D" first="Dan" last="Dou">Dan Dou</name><affiliation wicri:level="4"><nlm:aff id="aff1">From the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden</nlm:aff><country xml:lang="fr">Suède</country><wicri:regionArea>From the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm</wicri:regionArea><orgName type="university">Université de Stockholm</orgName><placeName><settlement type="city">Stockholm</settlement><region nuts="1">Svealand</region><region nuts="1">Comté de Stockholm</region></placeName></affiliation></author><author><name sortKey="Daniels, Robert" sort="Daniels, Robert" uniqKey="Daniels R" first="Robert" last="Daniels">Robert Daniels</name><affiliation wicri:level="4"><nlm:aff id="aff1">From the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden</nlm:aff><country xml:lang="fr">Suède</country><wicri:regionArea>From the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm</wicri:regionArea><orgName type="university">Université de Stockholm</orgName><placeName><settlement type="city">Stockholm</settlement><region nuts="1">Svealand</region><region nuts="1">Comté de Stockholm</region></placeName></affiliation></author></analytic><series><title level="j">The Journal of Biological Chemistry</title><idno type="ISSN">0021-9258</idno><idno type="eISSN">1083-351X</idno><imprint><date when="2013">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><bold>Background:</bold> Transmembrane domain (TMD) interactions in bitopic proteins are less understood than in multispanning proteins.</p><p><bold>Results:</bold> The interaction of the neuraminidase TMDs from influenza A viruses increases with decreasing hydrophobicity.</p><p><bold>Conclusion:</bold> Neuraminidase TMD interactions are dependent on the helix localization and positioning of their polar residues in the membrane bilayer.</p><p><bold>Significance:</bold> Polar-mediated TMD interactions are related to their membrane-integration properties.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Biol Chem</journal-id><journal-id journal-id-type="iso-abbrev">J. Biol. Chem</journal-id><journal-id journal-id-type="hwp">jbc</journal-id><journal-id journal-id-type="pmc">jbc</journal-id><journal-id journal-id-type="publisher-id">JBC</journal-id><journal-title-group><journal-title>The Journal of Biological Chemistry</journal-title></journal-title-group><issn pub-type="ppub">0021-9258</issn><issn pub-type="epub">1083-351X</issn><publisher><publisher-name>American Society for Biochemistry and Molecular Biology</publisher-name><publisher-loc>9650 Rockville Pike, Bethesda, MD 20814, U.S.A.</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">23447533</article-id><article-id pub-id-type="pmc">3624445</article-id><article-id pub-id-type="publisher-id">M112.440230</article-id><article-id pub-id-type="doi">10.1074/jbc.M112.440230</article-id><article-categories><subj-group subj-group-type="heading"><subject>Membrane Biology</subject></subj-group></article-categories><title-group><article-title>Polar Residues and Their Positional Context Dictate the Transmembrane Domain Interactions of Influenza A Neuraminidases<xref ref-type="fn" rid="FN1">*</xref></article-title><alt-title alt-title-type="short">Amphipathicity Dictates Neuraminidase Transmembrane Domain Interactions</alt-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Nordholm</surname><given-names>Johan</given-names></name><xref ref-type="aff" rid="aff1"></xref><xref ref-type="author-notes" rid="FN2"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>da Silva</surname><given-names>Diogo V.</given-names></name><xref ref-type="aff" rid="aff1"></xref><xref ref-type="author-notes" rid="FN2"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Damjanovic</surname><given-names>Justina</given-names></name><xref ref-type="aff" rid="aff1"></xref></contrib><contrib contrib-type="author"><name><surname>Dou</surname><given-names>Dan</given-names></name><xref ref-type="aff" rid="aff1"></xref></contrib><contrib contrib-type="author"><name><surname>Daniels</surname><given-names>Robert</given-names></name><xref ref-type="aff" rid="aff1"></xref><xref ref-type="corresp" rid="cor1"><sup>2</sup></xref></contrib><aff id="aff1">From the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden</aff></contrib-group><author-notes><corresp id="cor1"><label>2</label> To whom correspondence should be addressed. Tel.: <phone>46-8-162460</phone>; Fax: <fax>46-8-153679</fax>; E-mail: <email>robertd@dbb.su.se</email>.</corresp><fn fn-type="equal" id="FN2"><label>1</label><p>Both authors contributed equally to this work.</p></fn></author-notes><pub-date pub-type="ppub"><day>12</day><month>4</month><year>2013</year></pub-date><pub-date pub-type="epub"><day>27</day><month>2</month><year>2013</year></pub-date><volume>288</volume><issue>15</issue><fpage>10652</fpage><lpage>10660</lpage><history><date date-type="received"><day>27</day><month>11</month><year>2012</year></date><date date-type="rev-recd"><day>26</day><month>2</month><year>2013</year></date></history><permissions><copyright-statement>© 2013 by The American Society for Biochemistry and Molecular Biology, Inc.</copyright-statement><copyright-year>2013</copyright-year></permissions><self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zbc01513010652.pdf"></self-uri><abstract abstract-type="teaser"><p><bold>Background:</bold> Transmembrane domain (TMD) interactions in bitopic proteins are less understood than in multispanning proteins.</p><p><bold>Results:</bold> The interaction of the neuraminidase TMDs from influenza A viruses increases with decreasing hydrophobicity.</p><p><bold>Conclusion:</bold> Neuraminidase TMD interactions are dependent on the helix localization and positioning of their polar residues in the membrane bilayer.</p><p><bold>Significance:</bold> Polar-mediated TMD interactions are related to their membrane-integration properties.</p></abstract><abstract><p>Interactions that facilitate transmembrane domain (TMD) dimerization have been identified mainly using synthetic TMDs. Here, we investigated how inherent properties within natural TMDs modulate their interaction strength by exploiting the sequence variation in the nine neuraminidase subtypes (N1–N9) and the prior knowledge that a N1 TMD oligomerizes. Initially, consensus TMDs were created from the influenza A virus database, and their interaction strengths were measured in a biological membrane system. The TMD interactions increased with respect to decreasing hydrophobicity across the subtypes (N1–N9) and within the human N1 subtype where the N1 TMDs from the pandemic H1N1 strain of swine origin were found to be significantly less hydrophobic. The hydrophobicity correlation was attributed to the conserved amphipathicity within the TMDs as the interactions were abolished by mutating residues on the polar faces that are unfavorably positioned in the membrane. Similarly, local changes enhanced the interactions only when a larger polar residue existed on the appropriate face in an unfavorable membrane position. Together, the analysis of this unique natural TMD data set demonstrates how polar-mediated TMD interactions from bitopic proteins depend on which polar residues are involved and their positioning with respect to the helix and the membrane bilayer.</p></abstract><kwd-group><kwd>Influenza Virus</kwd><kwd>Membrane</kwd><kwd>Membrane Biophysics</kwd><kwd>Membrane Proteins</kwd><kwd>Protein-Protein Interactions</kwd><kwd>Viral Protein</kwd><kwd>Amphipathic</kwd><kwd>Hydrophobicity</kwd><kwd>Polar Residues</kwd><kwd>Transmembrane Domains</kwd></kwd-group></article-meta></front></pmc><affiliations><list><country><li>Suède</li></country><region><li>Comté de Stockholm</li><li>Svealand</li></region><settlement><li>Stockholm</li></settlement><orgName><li>Université de Stockholm</li></orgName></list><tree><country name="Suède"><region name="Svealand"><name sortKey="Nordholm, Johan" sort="Nordholm, Johan" uniqKey="Nordholm J" first="Johan" last="Nordholm">Johan Nordholm</name></region><name sortKey="Da Silva, Diogo V" sort="Da Silva, Diogo V" uniqKey="Da Silva D" first="Diogo V." last="Da Silva">Diogo V. Da Silva</name><name sortKey="Damjanovic, Justina" sort="Damjanovic, Justina" uniqKey="Damjanovic J" first="Justina" last="Damjanovic">Justina Damjanovic</name><name sortKey="Daniels, Robert" sort="Daniels, Robert" uniqKey="Daniels R" first="Robert" last="Daniels">Robert Daniels</name><name sortKey="Dou, Dan" sort="Dou, Dan" uniqKey="Dou D" first="Dan" last="Dou">Dan Dou</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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