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Mapping of two O-GlcNAc modification sites in the capsid protein of the potyvirus Plum pox virus
A large number of O-linked N-acetylglucosamine ( O-GlcNAc) residues have been mapped in vertebrate proteins, however targets of O-GlcNAcylation in plants still have not been characterized. We show here that O-GlcNAcylation of the N-terminal region of the capsid protein of Plum pox virus resembles th...
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| Published in: | FEBS letters 2006-10, Vol.580 (25), p.5822-5828 |
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| creator | Pérez, José de Jesús Juárez, Silvia Chen, Dinghu Scott, Cheryl L. Hartweck, Lynn M. Olszewski, Neil E. García, Juan Antonio |
| description | A large number of
O-linked
N-acetylglucosamine (
O-GlcNAc) residues have been mapped in vertebrate proteins, however targets of
O-GlcNAcylation in plants still have not been characterized. We show here that
O-GlcNAcylation of the N-terminal region of the capsid protein of
Plum pox virus resembles that of animal proteins in introducing
O-GlcNAc monomers. Thr-19 and Thr-24 were specifically
O-GlcNAcylated. These residues are surrounded by amino acids typical of animal
O-GlcNAc acceptor sites, suggesting that the specificity of
O-GlcNAc transferases is conserved among plants and animals. In laboratory conditions, mutations preventing
O-GlcNAcylation of Thr-19 and Thr-24 did not have noticeable effects on PPV competence to infect
Prunus persicae or
Nicotiana clevelandii. However, the fact that Thr-19 and Thr-24 are highly conserved among different PPV strains suggests that their
O-GlcNAc modification could be relevant for efficient competitiveness in natural conditions. |
| doi_str_mv | 10.1016/j.febslet.2006.09.041 |
| format | article |
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O-linked
N-acetylglucosamine (
O-GlcNAc) residues have been mapped in vertebrate proteins, however targets of
O-GlcNAcylation in plants still have not been characterized. We show here that
O-GlcNAcylation of the N-terminal region of the capsid protein of
Plum pox virus resembles that of animal proteins in introducing
O-GlcNAc monomers. Thr-19 and Thr-24 were specifically
O-GlcNAcylated. These residues are surrounded by amino acids typical of animal
O-GlcNAc acceptor sites, suggesting that the specificity of
O-GlcNAc transferases is conserved among plants and animals. In laboratory conditions, mutations preventing
O-GlcNAcylation of Thr-19 and Thr-24 did not have noticeable effects on PPV competence to infect
Prunus persicae or
Nicotiana clevelandii. However, the fact that Thr-19 and Thr-24 are highly conserved among different PPV strains suggests that their
O-GlcNAc modification could be relevant for efficient competitiveness in natural conditions.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2006.09.041</identifier><identifier>PMID: 17014851</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Amino Acid Substitution ; Base Sequence ; Binding Sites ; Capsid protein ; Capsid Proteins - chemistry ; Capsid Proteins - genetics ; Capsid Proteins - metabolism ; days post infection ; DNA, Viral - genetics ; dpi ; Glycosylation ; MALDI-TOF ; Matrix-assisted Laser Desorption/Ionization-Time of Flight ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Nicotiana - virology ; Nicotiana clevelandii ; O-GlcNAc ; O-GlcNAc transferase ; O-GlcNAcylation ; O-glycosylation ; O-Linked N-acetylglucosamination ; O-linked β-N-acetylglucosamine ; OGT ; Plant Diseases - virology ; Plum pox virus ; Plum Pox Virus - chemistry ; Plum Pox Virus - genetics ; Plum Pox Virus - pathogenicity ; Potyvirus ; Protein Processing, Post-Translational ; Prunus ; Prunus - virology ; Recombinant Fusion Proteins - chemistry ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; SEC ; SECRET AGENT ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; SPINDLY ; SPY ; Threonine - chemistry</subject><ispartof>FEBS letters, 2006-10, Vol.580 (25), p.5822-5828</ispartof><rights>2006 Federation of European Biochemical Societies</rights><rights>FEBS Letters 580 (2006) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5063-91974fa8673873730f1321d99ff02c8349c2f165898783b3b2b4ba3f026d5cad3</citedby><cites>FETCH-LOGICAL-c5063-91974fa8673873730f1321d99ff02c8349c2f165898783b3b2b4ba3f026d5cad3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579306011513$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3549,27924,27925,45780</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17014851$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pérez, José de Jesús</creatorcontrib><creatorcontrib>Juárez, Silvia</creatorcontrib><creatorcontrib>Chen, Dinghu</creatorcontrib><creatorcontrib>Scott, Cheryl L.</creatorcontrib><creatorcontrib>Hartweck, Lynn M.</creatorcontrib><creatorcontrib>Olszewski, Neil E.</creatorcontrib><creatorcontrib>García, Juan Antonio</creatorcontrib><title>Mapping of two O-GlcNAc modification sites in the capsid protein of the potyvirus Plum pox virus</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>A large number of
O-linked
N-acetylglucosamine (
O-GlcNAc) residues have been mapped in vertebrate proteins, however targets of
O-GlcNAcylation in plants still have not been characterized. We show here that
O-GlcNAcylation of the N-terminal region of the capsid protein of
Plum pox virus resembles that of animal proteins in introducing
O-GlcNAc monomers. Thr-19 and Thr-24 were specifically
O-GlcNAcylated. These residues are surrounded by amino acids typical of animal
O-GlcNAc acceptor sites, suggesting that the specificity of
O-GlcNAc transferases is conserved among plants and animals. In laboratory conditions, mutations preventing
O-GlcNAcylation of Thr-19 and Thr-24 did not have noticeable effects on PPV competence to infect
Prunus persicae or
Nicotiana clevelandii. However, the fact that Thr-19 and Thr-24 are highly conserved among different PPV strains suggests that their
O-GlcNAc modification could be relevant for efficient competitiveness in natural conditions.</description><subject>Amino Acid Sequence</subject><subject>Amino Acid Substitution</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Capsid protein</subject><subject>Capsid Proteins - chemistry</subject><subject>Capsid Proteins - genetics</subject><subject>Capsid Proteins - metabolism</subject><subject>days post infection</subject><subject>DNA, Viral - genetics</subject><subject>dpi</subject><subject>Glycosylation</subject><subject>MALDI-TOF</subject><subject>Matrix-assisted Laser Desorption/Ionization-Time of Flight</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Nicotiana - virology</subject><subject>Nicotiana clevelandii</subject><subject>O-GlcNAc</subject><subject>O-GlcNAc transferase</subject><subject>O-GlcNAcylation</subject><subject>O-glycosylation</subject><subject>O-Linked N-acetylglucosamination</subject><subject>O-linked β-N-acetylglucosamine</subject><subject>OGT</subject><subject>Plant Diseases - virology</subject><subject>Plum pox virus</subject><subject>Plum Pox Virus - chemistry</subject><subject>Plum Pox Virus - genetics</subject><subject>Plum Pox Virus - pathogenicity</subject><subject>Potyvirus</subject><subject>Protein Processing, Post-Translational</subject><subject>Prunus</subject><subject>Prunus - virology</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>SEC</subject><subject>SECRET AGENT</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>SPINDLY</subject><subject>SPY</subject><subject>Threonine - chemistry</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><recordid>eNqNUU1v3SAQRFGj5jXNT0jFqTc7i7ExnKo0ypeUL6ntmWAMLU-2cQ1O-v59cN-TckxOaHZnZpdZhI4J5AQIO1nn1jShMzEvAFgOIoeS7KEV4TXNaMn4B7QCIGVW1YIeoE8hrCFhTsRHdEDq1OEVWaHHWzWObviNvcXx2eP77LLTd6ca97511mkVnR9wcNEE7AYc_xis1Rhci8fJR5NKizBVRx83T26aA37o5j7Bf_g__Iz2reqCOdq9h-jXxfnPs6vs5v7y-uz0JtMVMJoJIurSKs5qmj5QU7CEFqQVwlooNKel0IUlrOKC15w2tCmaslE0NVlbadXSQ_R165v2-jubEGXvgjZdpwbj5yCTP2EcykSstkQ9-RAmY-U4uV5NG0lALtHKtdxFK5doJQiZok26L7sBc9Ob9lW1yzIRrraEZ9eZzftc5cX59-LHcqflTMCAkOSUrL5trUxK7MmZSQbtzKBN6yajo2y9e2PbF-lBoaw</recordid><startdate>20061030</startdate><enddate>20061030</enddate><creator>Pérez, José de Jesús</creator><creator>Juárez, Silvia</creator><creator>Chen, Dinghu</creator><creator>Scott, Cheryl L.</creator><creator>Hartweck, Lynn M.</creator><creator>Olszewski, Neil E.</creator><creator>García, Juan Antonio</creator><general>Elsevier B.V</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><scope>7U9</scope><scope>H94</scope></search><sort><creationdate>20061030</creationdate><title>Mapping of two O-GlcNAc modification sites in the capsid protein of the potyvirus Plum pox virus</title><author>Pérez, José de Jesús ; Juárez, Silvia ; Chen, Dinghu ; Scott, Cheryl L. ; Hartweck, Lynn M. ; Olszewski, Neil E. ; García, Juan Antonio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5063-91974fa8673873730f1321d99ff02c8349c2f165898783b3b2b4ba3f026d5cad3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino Acid Sequence</topic><topic>Amino Acid Substitution</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Capsid protein</topic><topic>Capsid Proteins - chemistry</topic><topic>Capsid Proteins - genetics</topic><topic>Capsid Proteins - metabolism</topic><topic>days post infection</topic><topic>DNA, Viral - genetics</topic><topic>dpi</topic><topic>Glycosylation</topic><topic>MALDI-TOF</topic><topic>Matrix-assisted Laser Desorption/Ionization-Time of Flight</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Nicotiana - virology</topic><topic>Nicotiana clevelandii</topic><topic>O-GlcNAc</topic><topic>O-GlcNAc transferase</topic><topic>O-GlcNAcylation</topic><topic>O-glycosylation</topic><topic>O-Linked N-acetylglucosamination</topic><topic>O-linked β-N-acetylglucosamine</topic><topic>OGT</topic><topic>Plant Diseases - virology</topic><topic>Plum pox virus</topic><topic>Plum Pox Virus - chemistry</topic><topic>Plum Pox Virus - genetics</topic><topic>Plum Pox Virus - pathogenicity</topic><topic>Potyvirus</topic><topic>Protein Processing, Post-Translational</topic><topic>Prunus</topic><topic>Prunus - virology</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>SEC</topic><topic>SECRET AGENT</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>SPINDLY</topic><topic>SPY</topic><topic>Threonine - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pérez, José de Jesús</creatorcontrib><creatorcontrib>Juárez, Silvia</creatorcontrib><creatorcontrib>Chen, Dinghu</creatorcontrib><creatorcontrib>Scott, Cheryl L.</creatorcontrib><creatorcontrib>Hartweck, Lynn M.</creatorcontrib><creatorcontrib>Olszewski, Neil E.</creatorcontrib><creatorcontrib>García, Juan Antonio</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>Pérez, José de Jesús</au><au>Juárez, Silvia</au><au>Chen, Dinghu</au><au>Scott, Cheryl L.</au><au>Hartweck, Lynn M.</au><au>Olszewski, Neil E.</au><au>García, Juan Antonio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mapping of two O-GlcNAc modification sites in the capsid protein of the potyvirus Plum pox virus</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2006-10-30</date><risdate>2006</risdate><volume>580</volume><issue>25</issue><spage>5822</spage><epage>5828</epage><pages>5822-5828</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>A large number of
O-linked
N-acetylglucosamine (
O-GlcNAc) residues have been mapped in vertebrate proteins, however targets of
O-GlcNAcylation in plants still have not been characterized. We show here that
O-GlcNAcylation of the N-terminal region of the capsid protein of
Plum pox virus resembles that of animal proteins in introducing
O-GlcNAc monomers. Thr-19 and Thr-24 were specifically
O-GlcNAcylated. These residues are surrounded by amino acids typical of animal
O-GlcNAc acceptor sites, suggesting that the specificity of
O-GlcNAc transferases is conserved among plants and animals. In laboratory conditions, mutations preventing
O-GlcNAcylation of Thr-19 and Thr-24 did not have noticeable effects on PPV competence to infect
Prunus persicae or
Nicotiana clevelandii. However, the fact that Thr-19 and Thr-24 are highly conserved among different PPV strains suggests that their
O-GlcNAc modification could be relevant for efficient competitiveness in natural conditions.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>17014851</pmid><doi>10.1016/j.febslet.2006.09.041</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 2006-10, Vol.580 (25), p.5822-5828 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_19716804 |
| source | ScienceDirect; Wiley |
| subjects | Amino Acid Sequence Amino Acid Substitution Base Sequence Binding Sites Capsid protein Capsid Proteins - chemistry Capsid Proteins - genetics Capsid Proteins - metabolism days post infection DNA, Viral - genetics dpi Glycosylation MALDI-TOF Matrix-assisted Laser Desorption/Ionization-Time of Flight Molecular Sequence Data Mutagenesis, Site-Directed Nicotiana - virology Nicotiana clevelandii O-GlcNAc O-GlcNAc transferase O-GlcNAcylation O-glycosylation O-Linked N-acetylglucosamination O-linked β-N-acetylglucosamine OGT Plant Diseases - virology Plum pox virus Plum Pox Virus - chemistry Plum Pox Virus - genetics Plum Pox Virus - pathogenicity Potyvirus Protein Processing, Post-Translational Prunus Prunus - virology Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism SEC SECRET AGENT Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization SPINDLY SPY Threonine - chemistry |
| title | Mapping of two O-GlcNAc modification sites in the capsid protein of the potyvirus Plum pox virus |
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