Crystal Structure of ORF12 from Lactococcus lactis Phage p2 Identifies a Tape Measure Protein Chaperone
Identifieur interne : 002933 ( Main/Exploration ); précédent : 002932; suivant : 002934Crystal Structure of ORF12 from Lactococcus lactis Phage p2 Identifies a Tape Measure Protein Chaperone
Auteurs : Marina Siponen [France] ; Giuliano Sciara [France] ; Manuela Villion [Canada] ; Silvia Spinelli [France] ; Julie Lichiere [France] ; Christian Cambillau [France] ; Sylvain Moineau [Canada] ; Valérie Campanacci [France]Source :
- Journal of bacteriology [ 0021-9193 ] ; 2009.
Descripteurs français
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English descriptors
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Abstract
We report here the characterization of the nonstructural protein ORF12 of the virulent lactococcal phage p2, which belongs to the Siphoviridae family. ORF12 was produced as a soluble protein, which forms large oligomers (6- to 15-mers) in solution. Using anti-ORF12 antibodies, we have confirmed that ORF12 is not found in the virion structure but is detected in the second half of the lytic cycle, indicating that it is a late-expressed protein. The structure of ORF12, solved by single anomalous diffraction and refined at 2.9-Å resolution, revealed a previously unknown fold as well as the presence of a hydrophobic patch at its surface. Furthermore, crystal packing of ORF12 formed long spirals in which a hydrophobic, continuous crevice was identified. This crevice exhibited a repeated motif of aromatic residues, which coincided with the same repeated motif usually found in tape measure protein (TMP), predicted to form helices. A model of a complex between ORF12 and a repeated motif of the TMP of phage p2 (ORF14) was generated, in which the TMP helix fitted exquisitely in the crevice and the aromatic patches of ORF12. We suggest, therefore, that ORF12 might act as a chaperone for TMP hydrophobic repeats, maintaining TMP in solution during the tail assembly of the lactococcal siphophage p2.
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xml:lang="en" level="a">Crystal Structure of ORF12 from Lactococcus lactis Phage p2 Identifies a Tape Measure Protein Chaperone</title><author><name sortKey="Siponen, Marina" sort="Siponen, Marina" uniqKey="Siponen M" first="Marina" last="Siponen">Marina Siponen</name><affiliation wicri:level="3"><inist:fA14 i1="01"><s1>Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS and Universités d'Aix-Marseille I & II, Campus de Luminy, case 932</s1><s2>13288 Marseille</s2><s3>FRA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>8 aut.</sZ></inist:fA14><country>France</country><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">Marseille</settlement></placeName></affiliation></author><author><name sortKey="Sciara, Giuliano" sort="Sciara, Giuliano" uniqKey="Sciara G" first="Giuliano" last="Sciara">Giuliano Sciara</name><affiliation wicri:level="3"><inist:fA14 i1="01"><s1>Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS and Universités d'Aix-Marseille I & II, Campus de Luminy, case 932</s1><s2>13288 Marseille</s2><s3>FRA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>8 aut.</sZ></inist:fA14><country>France</country><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">Marseille</settlement></placeName></affiliation></author><author><name sortKey="Villion, Manuela" sort="Villion, Manuela" uniqKey="Villion M" first="Manuela" last="Villion">Manuela Villion</name><affiliation wicri:level="1"><inist:fA14 i1="02"><s1>Groupe de Recherche en Écologie Buccale (GREB), Faculté de Médecine Dentaire, Université Laval</s1><s2>Québec City, Québec, G1K 7P4</s2><s3>CAN</s3><sZ>3 aut.</sZ><sZ>7 aut.</sZ></inist:fA14><country>Canada</country><wicri:noRegion>Québec City, Québec, G1K 7P4</wicri:noRegion></affiliation><affiliation wicri:level="1"><inist:fA14 i1="03"><s1>Département de Biochimie et de Microbiologie, Faculté des Sciences et de Génie, Université Laval</s1><s2>Québec City, Québec, G1K 7P4</s2><s3>CAN</s3><sZ>3 aut.</sZ><sZ>7 aut.</sZ></inist:fA14><country>Canada</country><wicri:noRegion>Québec City, Québec, G1K 7P4</wicri:noRegion></affiliation></author><author><name sortKey="Spinelli, Silvia" sort="Spinelli, Silvia" uniqKey="Spinelli S" first="Silvia" last="Spinelli">Silvia Spinelli</name><affiliation wicri:level="3"><inist:fA14 i1="01"><s1>Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS and Universités d'Aix-Marseille I & II, Campus de Luminy, case 932</s1><s2>13288 Marseille</s2><s3>FRA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>8 aut.</sZ></inist:fA14><country>France</country><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">Marseille</settlement></placeName></affiliation></author><author><name sortKey="Lichiere, Julie" sort="Lichiere, Julie" uniqKey="Lichiere J" first="Julie" last="Lichiere">Julie Lichiere</name><affiliation wicri:level="3"><inist:fA14 i1="01"><s1>Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS and Universités d'Aix-Marseille I & II, Campus de Luminy, case 932</s1><s2>13288 Marseille</s2><s3>FRA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>8 aut.</sZ></inist:fA14><country>France</country><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">Marseille</settlement></placeName></affiliation></author><author><name sortKey="Cambillau, Christian" sort="Cambillau, Christian" uniqKey="Cambillau C" first="Christian" last="Cambillau">Christian Cambillau</name><affiliation wicri:level="3"><inist:fA14 i1="01"><s1>Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS and Universités d'Aix-Marseille I & II, Campus de Luminy, case 932</s1><s2>13288 Marseille</s2><s3>FRA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>8 aut.</sZ></inist:fA14><country>France</country><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">Marseille</settlement></placeName></affiliation></author><author><name sortKey="Moineau, Sylvain" sort="Moineau, Sylvain" uniqKey="Moineau S" first="Sylvain" last="Moineau">Sylvain Moineau</name><affiliation wicri:level="1"><inist:fA14 i1="02"><s1>Groupe de Recherche en Écologie Buccale (GREB), Faculté de Médecine Dentaire, Université Laval</s1><s2>Québec City, Québec, G1K 7P4</s2><s3>CAN</s3><sZ>3 aut.</sZ><sZ>7 aut.</sZ></inist:fA14><country>Canada</country><wicri:noRegion>Québec City, Québec, G1K 7P4</wicri:noRegion></affiliation><affiliation wicri:level="1"><inist:fA14 i1="03"><s1>Département de Biochimie et de Microbiologie, Faculté des Sciences et de Génie, Université Laval</s1><s2>Québec City, Québec, G1K 7P4</s2><s3>CAN</s3><sZ>3 aut.</sZ><sZ>7 aut.</sZ></inist:fA14><country>Canada</country><wicri:noRegion>Québec City, Québec, G1K 7P4</wicri:noRegion></affiliation><affiliation wicri:level="1"><inist:fA14 i1="04"><s1>Félix d'Hérelle Reference Center for Bacterial Viruses, Université Laval</s1><s2>Québec City, Québec, G1K 7P4</s2><s3>CAN</s3><sZ>7 aut.</sZ></inist:fA14><country>Canada</country><wicri:noRegion>Québec City, Québec, G1K 7P4</wicri:noRegion></affiliation></author><author><name sortKey="Campanacci, Valerie" sort="Campanacci, Valerie" uniqKey="Campanacci V" first="Valérie" last="Campanacci">Valérie Campanacci</name><affiliation wicri:level="3"><inist:fA14 i1="01"><s1>Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS and Universités d'Aix-Marseille I & II, Campus de Luminy, case 932</s1><s2>13288 Marseille</s2><s3>FRA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>8 aut.</sZ></inist:fA14><country>France</country><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">Marseille</settlement></placeName></affiliation></author></analytic><series><title level="j" type="main">Journal of bacteriology</title><title level="j" type="abbreviated">J. bacteriol.</title><idno type="ISSN">0021-9193</idno><imprint><date when="2009">2009</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Journal of bacteriology</title><title level="j" type="abbreviated">J. bacteriol.</title><idno type="ISSN">0021-9193</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Chaperone</term><term>Crystalline structure</term><term>Identification</term><term>Lactococcus lactis</term><term>Microbiology</term><term>Phage P2</term><term>Protein</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Lactococcus lactis</term><term>Bactériophage P2</term><term>Structure cristalline</term><term>Identification</term><term>Protéine</term><term>Chaperon</term><term>Microbiologie</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We report here the characterization of the nonstructural protein ORF12 of the virulent lactococcal phage p2, which belongs to the Siphoviridae family. ORF12 was produced as a soluble protein, which forms large oligomers (6- to 15-mers) in solution. Using anti-ORF12 antibodies, we have confirmed that ORF12 is not found in the virion structure but is detected in the second half of the lytic cycle, indicating that it is a late-expressed protein. The structure of ORF12, solved by single anomalous diffraction and refined at 2.9-Å resolution, revealed a previously unknown fold as well as the presence of a hydrophobic patch at its surface. Furthermore, crystal packing of ORF12 formed long spirals in which a hydrophobic, continuous crevice was identified. This crevice exhibited a repeated motif of aromatic residues, which coincided with the same repeated motif usually found in tape measure protein (TMP), predicted to form helices. A model of a complex between ORF12 and a repeated motif of the TMP of phage p2 (ORF14) was generated, in which the TMP helix fitted exquisitely in the crevice and the aromatic patches of ORF12. We suggest, therefore, that ORF12 might act as a chaperone for TMP hydrophobic repeats, maintaining TMP in solution during the tail assembly of the lactococcal siphophage p2.</div></front></TEI><affiliations><list><country><li>Canada</li><li>France</li></country><region><li>Provence-Alpes-Côte d'Azur</li></region><settlement><li>Marseille</li></settlement></list><tree><country name="France"><region name="Provence-Alpes-Côte d'Azur"><name sortKey="Siponen, Marina" sort="Siponen, Marina" uniqKey="Siponen M" first="Marina" last="Siponen">Marina Siponen</name></region><name sortKey="Cambillau, Christian" sort="Cambillau, Christian" uniqKey="Cambillau C" first="Christian" last="Cambillau">Christian Cambillau</name><name sortKey="Campanacci, Valerie" sort="Campanacci, Valerie" uniqKey="Campanacci V" first="Valérie" last="Campanacci">Valérie Campanacci</name><name sortKey="Lichiere, Julie" sort="Lichiere, Julie" uniqKey="Lichiere J" first="Julie" last="Lichiere">Julie Lichiere</name><name sortKey="Sciara, Giuliano" sort="Sciara, Giuliano" uniqKey="Sciara G" first="Giuliano" last="Sciara">Giuliano Sciara</name><name sortKey="Spinelli, Silvia" sort="Spinelli, Silvia" uniqKey="Spinelli S" first="Silvia" last="Spinelli">Silvia Spinelli</name></country><country name="Canada"><noRegion><name sortKey="Villion, Manuela" sort="Villion, Manuela" uniqKey="Villion M" first="Manuela" last="Villion">Manuela Villion</name></noRegion><name sortKey="Moineau, Sylvain" sort="Moineau, Sylvain" uniqKey="Moineau S" first="Sylvain" last="Moineau">Sylvain Moineau</name><name sortKey="Moineau, Sylvain" sort="Moineau, Sylvain" uniqKey="Moineau S" first="Sylvain" last="Moineau">Sylvain Moineau</name><name sortKey="Moineau, Sylvain" sort="Moineau, Sylvain" uniqKey="Moineau S" first="Sylvain" last="Moineau">Sylvain Moineau</name><name sortKey="Villion, Manuela" sort="Villion, Manuela" uniqKey="Villion M" first="Manuela" last="Villion">Manuela Villion</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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