Crystal Structure of ORF12 from Lactococcus lactis Phage p2 Identifies a Tape Measure Protein Chaperone
Identifieur interne : 000026 ( PascalFrancis/Curation ); précédent : 000025; suivant : 000027Crystal 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.
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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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aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>8 aut.</sZ></inist:fA14><country>France</country></affiliation></author><author><name sortKey="Sciara, Giuliano" sort="Sciara, Giuliano" uniqKey="Sciara G" first="Giuliano" last="Sciara">Giuliano Sciara</name><affiliation wicri:level="1"><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></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></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></affiliation></author><author><name sortKey="Spinelli, Silvia" sort="Spinelli, Silvia" uniqKey="Spinelli S" first="Silvia" last="Spinelli">Silvia Spinelli</name><affiliation wicri:level="1"><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></affiliation></author><author><name sortKey="Lichiere, Julie" sort="Lichiere, Julie" uniqKey="Lichiere J" first="Julie" last="Lichiere">Julie Lichiere</name><affiliation wicri:level="1"><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></affiliation></author><author><name sortKey="Cambillau, Christian" sort="Cambillau, Christian" uniqKey="Cambillau C" first="Christian" last="Cambillau">Christian Cambillau</name><affiliation wicri:level="1"><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></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></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></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></affiliation></author><author><name sortKey="Campanacci, Valerie" sort="Campanacci, Valerie" uniqKey="Campanacci V" first="Valérie" last="Campanacci">Valérie Campanacci</name><affiliation wicri:level="1"><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></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><inist><standard h6="B"><pA><fA01 i1="01" i2="1"><s0>0021-9193</s0></fA01><fA02 i1="01"><s0>JOBAAY</s0></fA02><fA03 i2="1"><s0>J. bacteriol.</s0></fA03><fA05><s2>191</s2></fA05><fA06><s2>3</s2></fA06><fA08 i1="01" i2="1" l="ENG"><s1>Crystal Structure of ORF12 from Lactococcus lactis Phage p2 Identifies a Tape Measure Protein Chaperone</s1></fA08><fA11 i1="01" i2="1"><s1>SIPONEN (Marina)</s1></fA11><fA11 i1="02" i2="1"><s1>SCIARA (Giuliano)</s1></fA11><fA11 i1="03" i2="1"><s1>VILLION (Manuela)</s1></fA11><fA11 i1="04" i2="1"><s1>SPINELLI (Silvia)</s1></fA11><fA11 i1="05" i2="1"><s1>LICHIERE (Julie)</s1></fA11><fA11 i1="06" i2="1"><s1>CAMBILLAU (Christian)</s1></fA11><fA11 i1="07" i2="1"><s1>MOINEAU (Sylvain)</s1></fA11><fA11 i1="08" i2="1"><s1>CAMPANACCI (Valérie)</s1></fA11><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></fA14><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></fA14><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></fA14><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></fA14><fA20><s1>728-734</s1></fA20><fA21><s1>2009</s1></fA21><fA23 i1="01"><s0>ENG</s0></fA23><fA43 i1="01"><s1>INIST</s1><s2>2041</s2><s5>354000184199610080</s5></fA43><fA44><s0>0000</s0><s1>© 2009 INIST-CNRS. All rights reserved.</s1></fA44><fA45><s0>47 ref.</s0></fA45><fA47 i1="01" i2="1"><s0>09-0106916</s0></fA47><fA60><s1>P</s1></fA60><fA61><s0>A</s0></fA61><fA64 i1="01" i2="1"><s0>Journal of bacteriology</s0></fA64><fA66 i1="01"><s0>USA</s0></fA66><fC01 i1="01" l="ENG"><s0>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.</s0></fC01><fC02 i1="01" i2="X"><s0>002A05B15</s0></fC02><fC02 i1="02" i2="X"><s0>002A05C10</s0></fC02><fC03 i1="01" i2="X" l="FRE"><s0>Lactococcus lactis</s0><s2>NS</s2><s5>01</s5></fC03><fC03 i1="01" i2="X" l="ENG"><s0>Lactococcus lactis</s0><s2>NS</s2><s5>01</s5></fC03><fC03 i1="01" i2="X" l="SPA"><s0>Lactococcus lactis</s0><s2>NS</s2><s5>01</s5></fC03><fC03 i1="02" i2="X" l="FRE"><s0>Bactériophage P2</s0><s2>NW</s2><s5>02</s5></fC03><fC03 i1="02" i2="X" l="ENG"><s0>Phage P2</s0><s2>NW</s2><s5>02</s5></fC03><fC03 i1="02" i2="X" l="SPA"><s0>Phage P2</s0><s2>NW</s2><s5>02</s5></fC03><fC03 i1="03" i2="X" l="FRE"><s0>Structure cristalline</s0><s5>05</s5></fC03><fC03 i1="03" i2="X" l="ENG"><s0>Crystalline structure</s0><s5>05</s5></fC03><fC03 i1="03" i2="X" l="SPA"><s0>Estructura cristalina</s0><s5>05</s5></fC03><fC03 i1="04" i2="X" l="FRE"><s0>Identification</s0><s5>06</s5></fC03><fC03 i1="04" i2="X" l="ENG"><s0>Identification</s0><s5>06</s5></fC03><fC03 i1="04" i2="X" l="SPA"><s0>Identificación</s0><s5>06</s5></fC03><fC03 i1="05" i2="X" l="FRE"><s0>Protéine</s0><s5>07</s5></fC03><fC03 i1="05" i2="X" l="ENG"><s0>Protein</s0><s5>07</s5></fC03><fC03 i1="05" i2="X" l="SPA"><s0>Proteína</s0><s5>07</s5></fC03><fC03 i1="06" i2="X" l="FRE"><s0>Chaperon</s0><s5>08</s5></fC03><fC03 i1="06" i2="X" l="ENG"><s0>Chaperone</s0><s5>08</s5></fC03><fC03 i1="06" i2="X" l="SPA"><s0>Chaperone</s0><s5>08</s5></fC03><fC03 i1="07" i2="X" l="FRE"><s0>Microbiologie</s0><s5>09</s5></fC03><fC03 i1="07" i2="X" l="ENG"><s0>Microbiology</s0><s5>09</s5></fC03><fC03 i1="07" i2="X" l="SPA"><s0>Microbiología</s0><s5>09</s5></fC03><fC07 i1="01" i2="X" l="FRE"><s0>Streptococcaceae</s0><s2>NS</s2></fC07><fC07 i1="01" i2="X" l="ENG"><s0>Streptococcaceae</s0><s2>NS</s2></fC07><fC07 i1="01" i2="X" l="SPA"><s0>Streptococcaceae</s0><s2>NS</s2></fC07><fC07 i1="02" i2="X" l="FRE"><s0>Micrococcales</s0><s2>NS</s2></fC07><fC07 i1="02" i2="X" l="ENG"><s0>Micrococcales</s0><s2>NS</s2></fC07><fC07 i1="02" i2="X" l="SPA"><s0>Micrococcales</s0><s2>NS</s2></fC07><fC07 i1="03" i2="X" l="FRE"><s0>Bactérie</s0></fC07><fC07 i1="03" i2="X" l="ENG"><s0>Bacteria</s0></fC07><fC07 i1="03" i2="X" l="SPA"><s0>Bacteria</s0></fC07><fC07 i1="04" i2="X" l="FRE"><s0>Bactériophage</s0><s2>NW</s2></fC07><fC07 i1="04" i2="X" l="ENG"><s0>Phage</s0><s2>NW</s2></fC07><fC07 i1="04" i2="X" l="SPA"><s0>Phage</s0><s2>NW</s2></fC07><fC07 i1="05" i2="X" l="FRE"><s0>Virus</s0><s2>NW</s2></fC07><fC07 i1="05" i2="X" l="ENG"><s0>Virus</s0><s2>NW</s2></fC07><fC07 i1="05" i2="X" l="SPA"><s0>Virus</s0><s2>NW</s2></fC07><fC07 i1="06" i2="X" l="FRE"><s0>Bactérie lactique</s0><s5>13</s5></fC07><fC07 i1="06" i2="X" l="ENG"><s0>Lactic acid bacteria</s0><s5>13</s5></fC07><fC07 i1="06" i2="X" l="SPA"><s0>Bacteria láctica</s0><s5>13</s5></fC07><fN21><s1>075</s1></fN21><fN44 i1="01"><s1>OTO</s1></fN44><fN82><s1>OTO</s1></fN82></pA></standard></inist></record>Pour manipuler ce document sous Unix (Dilib)
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|texte= Crystal Structure of ORF12 from Lactococcus lactis Phage p2 Identifies a Tape Measure Protein Chaperone
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