Structure-function analysis of severe acute respiratory syndrome coronavirus RNA cap guanine-N7-methyltransferase.
Identifieur interne : 001853 ( Main/Exploration ); précédent : 001852; suivant : 001854Structure-function analysis of severe acute respiratory syndrome coronavirus RNA cap guanine-N7-methyltransferase.
Auteurs : Yu Chen [République populaire de Chine] ; Jiali Tao ; Ying Sun ; Andong Wu ; Ceyang Su ; Guozhen Gao ; Hui Cai ; Su Qiu ; Yingliang Wu ; Tero Ahola ; Deyin GuoSource :
- Journal of virology [ 1098-5514 ] ; 2013.
Descripteurs français
- KwdFr :
- ARN viral (génétique), ARN viral (métabolisme), Coiffes des ARN (génétique), Coiffes des ARN (métabolisme), Exoribonucleases (), Exoribonucleases (génétique), Exoribonucleases (métabolisme), Methyltransferases (), Methyltransferases (génétique), Methyltransferases (métabolisme), Méthylation, Protéines virales (), Protéines virales (génétique), Protéines virales (métabolisme), Protéines virales non structurales (), Protéines virales non structurales (génétique), Protéines virales non structurales (métabolisme), Structure tertiaire des protéines, Syndrome respiratoire aigu sévère (virologie), Virus du SRAS (), Virus du SRAS (enzymologie), Virus du SRAS (génétique), Virus du SRAS (métabolisme).
- MESH :
- enzymologie : Virus du SRAS.
- génétique : ARN viral, Coiffes des ARN, Exoribonucleases, Methyltransferases, Protéines virales, Protéines virales non structurales, Virus du SRAS.
- métabolisme : ARN viral, Coiffes des ARN, Exoribonucleases, Methyltransferases, Protéines virales, Protéines virales non structurales, Virus du SRAS.
- virologie : Syndrome respiratoire aigu sévère.
- Exoribonucleases, Methyltransferases, Méthylation, Protéines virales, Protéines virales non structurales, Structure tertiaire des protéines, Virus du SRAS.
English descriptors
- KwdEn :
- Exoribonucleases (chemistry), Exoribonucleases (genetics), Exoribonucleases (metabolism), Methylation, Methyltransferases (chemistry), Methyltransferases (genetics), Methyltransferases (metabolism), Protein Structure, Tertiary, RNA Caps (genetics), RNA Caps (metabolism), RNA, Viral (genetics), RNA, Viral (metabolism), SARS Virus (chemistry), SARS Virus (enzymology), SARS Virus (genetics), SARS Virus (metabolism), Severe Acute Respiratory Syndrome (virology), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism), Viral Proteins (chemistry), Viral Proteins (genetics), Viral Proteins (metabolism).
- MESH :
- chemical , chemistry : Exoribonucleases, Methyltransferases, Viral Nonstructural Proteins, Viral Proteins.
- chemical , genetics : Exoribonucleases, Methyltransferases, RNA Caps, RNA, Viral, Viral Nonstructural Proteins, Viral Proteins.
- chemical , metabolism : Exoribonucleases, Methyltransferases, RNA Caps, RNA, Viral, Viral Nonstructural Proteins, Viral Proteins.
- chemistry : SARS Virus.
- enzymology : SARS Virus.
- genetics : SARS Virus.
- metabolism : SARS Virus.
- virology : Severe Acute Respiratory Syndrome.
- Methylation, Protein Structure, Tertiary.
Abstract
Coronaviruses possess a cap structure at the 5' ends of viral genomic RNA and subgenomic RNAs, which is generated through consecutive methylations by virally encoded guanine-N7-methyltransferase (N7-MTase) and 2'-O-methyltransferase (2'-O-MTase). The coronaviral N7-MTase is unique for its physical linkage with an exoribonuclease (ExoN) harbored in nonstructural protein 14 (nsp14) of coronaviruses. In this study, the structure-function relationships of the N7-MTase were analyzed by deletion and site-directed mutagenesis of severe acute respiratory syndrome coronavirus (SARS-CoV) nsp14. The results showed that the ExoN domain is closely involved in the activity of the N7-MTase, suggesting that coronavirus N7-MTase is different from all other viral N7-MTases, which are separable from other structural domains located in the same polypeptide. Two of the 12 critical residues identified to be essential for the N7-MTase were located at the N terminus of the core ExoN domain, reinforcing a role of the ExoN domain in the N7-MTase activity of nsp14. The other 10 critical residues were distributed throughout the N7-MTase domain but localized mainly in the S-adenosyl-l-methionine (SAM)-binding pocket and key structural elements of the MTase fold of nsp14. The sequence motif DxGxPxA (amino acids [aa] 331 to 338) was identified as the key part of the SAM-binding site. These results provide insights into the structure and functional mechanisms of coronaviral nsp14 N7-MTase.
DOI: 10.1128/JVI.00061-13
PubMed: 23536667
Affiliations:
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(virology)</term><term>Viral Nonstructural Proteins (chemistry)</term><term>Viral Nonstructural Proteins (genetics)</term><term>Viral Nonstructural Proteins (metabolism)</term><term>Viral Proteins (chemistry)</term><term>Viral Proteins (genetics)</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN viral (génétique)</term><term>ARN viral (métabolisme)</term><term>Coiffes des ARN (génétique)</term><term>Coiffes des ARN (métabolisme)</term><term>Exoribonucleases ()</term><term>Exoribonucleases (génétique)</term><term>Exoribonucleases (métabolisme)</term><term>Methyltransferases ()</term><term>Methyltransferases (génétique)</term><term>Methyltransferases (métabolisme)</term><term>Méthylation</term><term>Protéines virales ()</term><term>Protéines virales (génétique)</term><term>Protéines virales (métabolisme)</term><term>Protéines virales non structurales ()</term><term>Protéines virales non structurales (génétique)</term><term>Protéines virales non structurales (métabolisme)</term><term>Structure tertiaire des protéines</term><term>Syndrome respiratoire aigu sévère (virologie)</term><term>Virus du SRAS ()</term><term>Virus du SRAS (enzymologie)</term><term>Virus du SRAS (génétique)</term><term>Virus du SRAS (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Exoribonucleases</term><term>Methyltransferases</term><term>Viral Nonstructural Proteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Exoribonucleases</term><term>Methyltransferases</term><term>RNA Caps</term><term>RNA, Viral</term><term>Viral Nonstructural Proteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Exoribonucleases</term><term>Methyltransferases</term><term>RNA Caps</term><term>RNA, Viral</term><term>Viral Nonstructural Proteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ARN viral</term><term>Coiffes des ARN</term><term>Exoribonucleases</term><term>Methyltransferases</term><term>Protéines virales</term><term>Protéines virales non structurales</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ARN viral</term><term>Coiffes des ARN</term><term>Exoribonucleases</term><term>Methyltransferases</term><term>Protéines virales</term><term>Protéines virales non structurales</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Methylation</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Exoribonucleases</term><term>Methyltransferases</term><term>Méthylation</term><term>Protéines virales</term><term>Protéines virales non structurales</term><term>Structure tertiaire des protéines</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Coronaviruses possess a cap structure at the 5' ends of viral genomic RNA and subgenomic RNAs, which is generated through consecutive methylations by virally encoded guanine-N7-methyltransferase (N7-MTase) and 2'-O-methyltransferase (2'-O-MTase). The coronaviral N7-MTase is unique for its physical linkage with an exoribonuclease (ExoN) harbored in nonstructural protein 14 (nsp14) of coronaviruses. In this study, the structure-function relationships of the N7-MTase were analyzed by deletion and site-directed mutagenesis of severe acute respiratory syndrome coronavirus (SARS-CoV) nsp14. The results showed that the ExoN domain is closely involved in the activity of the N7-MTase, suggesting that coronavirus N7-MTase is different from all other viral N7-MTases, which are separable from other structural domains located in the same polypeptide. Two of the 12 critical residues identified to be essential for the N7-MTase were located at the N terminus of the core ExoN domain, reinforcing a role of the ExoN domain in the N7-MTase activity of nsp14. The other 10 critical residues were distributed throughout the N7-MTase domain but localized mainly in the S-adenosyl-l-methionine (SAM)-binding pocket and key structural elements of the MTase fold of nsp14. The sequence motif DxGxPxA (amino acids [aa] 331 to 338) was identified as the key part of the SAM-binding site. These results provide insights into the structure and functional mechanisms of coronaviral nsp14 N7-MTase.</div></front></TEI><affiliations><list><country><li>République populaire de Chine</li></country><region><li>Hubei</li></region><settlement><li>Wuhan</li></settlement><orgName><li>Université de Wuhan</li></orgName></list><tree><noCountry><name sortKey="Ahola, Tero" sort="Ahola, Tero" uniqKey="Ahola T" first="Tero" last="Ahola">Tero Ahola</name><name sortKey="Cai, Hui" sort="Cai, Hui" uniqKey="Cai H" first="Hui" last="Cai">Hui Cai</name><name sortKey="Gao, Guozhen" sort="Gao, Guozhen" uniqKey="Gao G" first="Guozhen" last="Gao">Guozhen Gao</name><name sortKey="Guo, Deyin" sort="Guo, Deyin" uniqKey="Guo D" first="Deyin" last="Guo">Deyin Guo</name><name sortKey="Qiu, Su" sort="Qiu, Su" uniqKey="Qiu S" first="Su" last="Qiu">Su Qiu</name><name sortKey="Su, Ceyang" sort="Su, Ceyang" uniqKey="Su C" first="Ceyang" last="Su">Ceyang Su</name><name sortKey="Sun, Ying" sort="Sun, Ying" uniqKey="Sun Y" first="Ying" last="Sun">Ying Sun</name><name sortKey="Tao, Jiali" sort="Tao, Jiali" uniqKey="Tao J" first="Jiali" last="Tao">Jiali Tao</name><name sortKey="Wu, Andong" sort="Wu, Andong" uniqKey="Wu A" first="Andong" last="Wu">Andong Wu</name><name sortKey="Wu, Yingliang" sort="Wu, Yingliang" uniqKey="Wu Y" first="Yingliang" last="Wu">Yingliang Wu</name></noCountry><country name="République populaire de Chine"><region name="Hubei"><name sortKey="Chen, Yu" sort="Chen, Yu" uniqKey="Chen Y" first="Yu" last="Chen">Yu Chen</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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