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One severe acute respiratory syndrome coronavirus protein complex integrates processive RNA polymerase and exonuclease activities.

Identifieur interne : 000F36 ( PubMed/Curation ); précédent : 000F35; suivant : 000F37

One severe acute respiratory syndrome coronavirus protein complex integrates processive RNA polymerase and exonuclease activities.

Auteurs : Lorenzo Subissi [France] ; Clara C. Posthuma ; Axelle Collet [France] ; Jessika C. Zevenhoven-Dobbe ; Alexander E. Gorbalenya [Russie] ; Etienne Decroly [France] ; Eric J. Snijder ; Bruno Canard [France] ; Isabelle Imbert [France]

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2014.

RBID : pubmed:25197083

Descripteurs français

KwdFr :
- ARN (métabolisme), ARN viral (biosynthèse), Biocatalyse, Complexes multiprotéiques (métabolisme), DNA-directed RNA polymerases (métabolisme), Données de séquences moléculaires, Exoribonucleases (métabolisme), Génétique inverse, Humains, Liaison aux protéines, Mutation (génétique), Protéines mutantes (métabolisme), Protéines virales non structurales (métabolisme), Reproductibilité des résultats, Réplication virale, Syndrome respiratoire aigu sévère (virologie), Séquence nucléotidique, Virus du SRAS (métabolisme).
MESH :
- biosynthèse : ARN viral.
- génétique : Mutation.
- métabolisme : ARN, Complexes multiprotéiques, DNA-directed RNA polymerases, Exoribonucleases, Protéines mutantes, Protéines virales non structurales, Virus du SRAS.
- virologie : Syndrome respiratoire aigu sévère.
- Biocatalyse, Données de séquences moléculaires, Génétique inverse, Humains, Liaison aux protéines, Reproductibilité des résultats, Réplication virale, Séquence nucléotidique.

English descriptors

KwdEn :
- Base Sequence, Biocatalysis, DNA-Directed RNA Polymerases (metabolism), Exoribonucleases (metabolism), Humans, Molecular Sequence Data, Multiprotein Complexes (metabolism), Mutant Proteins (metabolism), Mutation (genetics), Protein Binding, RNA (metabolism), RNA, Viral (biosynthesis), Reproducibility of Results, Reverse Genetics, SARS Virus (metabolism), Severe Acute Respiratory Syndrome (virology), Viral Nonstructural Proteins (metabolism), Virus Replication.
MESH :
- chemical , biosynthesis : RNA, Viral.
- chemical , metabolism : DNA-Directed RNA Polymerases, Exoribonucleases, Multiprotein Complexes, Mutant Proteins, RNA, Viral Nonstructural Proteins.
- genetics : Mutation.
- metabolism : SARS Virus.
- virology : Severe Acute Respiratory Syndrome.
- Base Sequence, Biocatalysis, Humans, Molecular Sequence Data, Protein Binding, Reproducibility of Results, Reverse Genetics, Virus Replication.

Abstract

In addition to members causing milder human infections, the Coronaviridae family includes potentially lethal zoonotic agents causing severe acute respiratory syndrome (SARS) and the recently emerged Middle East respiratory syndrome. The ∼30-kb positive-stranded RNA genome of coronaviruses encodes a replication/transcription machinery that is unusually complex and composed of 16 nonstructural proteins (nsps). SARS-CoV nsp12, the canonical RNA-dependent RNA polymerase (RdRp), exhibits poorly processive RNA synthesis in vitro, at odds with the efficient replication of a very large RNA genome in vivo. Here, we report that SARS-CoV nsp7 and nsp8 activate and confer processivity to the RNA-synthesizing activity of nsp12. Using biochemical assays and reverse genetics, the importance of conserved nsp7 and nsp8 residues was probed. Whereas several nsp7 mutations affected virus replication to a limited extent, the replacement of two nsp8 residues (P183 and R190) essential for interaction with nsp12 and a third (K58) critical for the interaction of the polymerase complex with RNA were all lethal to the virus. Without a loss of processivity, the nsp7/nsp8/nsp12 complex can associate with nsp14, a bifunctional enzyme bearing 3'-5' exoribonuclease and RNA cap N7-guanine methyltransferase activities involved in replication fidelity and 5'-RNA capping, respectively. The identification of this tripartite polymerase complex that in turn associates with the nsp14 proofreading enzyme sheds light on how coronaviruses assemble an RNA-synthesizing machinery to replicate the largest known RNA genomes. This protein complex is a fascinating example of the functional integration of RNA polymerase, capping, and proofreading activities.

DOI: 10.1073/pnas.1323705111
PubMed: 25197083

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Clara C. Posthuma

<affiliation><nlm:affiliation>Molecular Virology Laboratory, Department of Medical Microbiology, Leiden University Medical Center, 2300RC, Leiden, The Netherlands; and.</nlm:affiliation>
<wicri:noCountry code="subField">The Netherlands; and</wicri:noCountry>
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Jessika C. Zevenhoven-Dobbe

<affiliation><nlm:affiliation>Molecular Virology Laboratory, Department of Medical Microbiology, Leiden University Medical Center, 2300RC, Leiden, The Netherlands; and.</nlm:affiliation>
<wicri:noCountry code="subField">The Netherlands; and</wicri:noCountry>
</affiliation>

Eric J. Snijder

<affiliation><nlm:affiliation>Molecular Virology Laboratory, Department of Medical Microbiology, Leiden University Medical Center, 2300RC, Leiden, The Netherlands; and.</nlm:affiliation>
<wicri:noCountry code="subField">The Netherlands; and</wicri:noCountry>
</affiliation>

Le document en format XML

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<term>Humans</term>
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<term>Mutant Proteins (metabolism)</term>
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<front><div type="abstract" xml:lang="en">In addition to members causing milder human infections, the Coronaviridae family includes potentially lethal zoonotic agents causing severe acute respiratory syndrome (SARS) and the recently emerged Middle East respiratory syndrome. The ∼30-kb positive-stranded RNA genome of coronaviruses encodes a replication/transcription machinery that is unusually complex and composed of 16 nonstructural proteins (nsps). SARS-CoV nsp12, the canonical RNA-dependent RNA polymerase (RdRp), exhibits poorly processive RNA synthesis in vitro, at odds with the efficient replication of a very large RNA genome in vivo. Here, we report that SARS-CoV nsp7 and nsp8 activate and confer processivity to the RNA-synthesizing activity of nsp12. Using biochemical assays and reverse genetics, the importance of conserved nsp7 and nsp8 residues was probed. Whereas several nsp7 mutations affected virus replication to a limited extent, the replacement of two nsp8 residues (P183 and R190) essential for interaction with nsp12 and a third (K58) critical for the interaction of the polymerase complex with RNA were all lethal to the virus. Without a loss of processivity, the nsp7/nsp8/nsp12 complex can associate with nsp14, a bifunctional enzyme bearing 3'-5' exoribonuclease and RNA cap N7-guanine methyltransferase activities involved in replication fidelity and 5'-RNA capping, respectively. The identification of this tripartite polymerase complex that in turn associates with the nsp14 proofreading enzyme sheds light on how coronaviruses assemble an RNA-synthesizing machinery to replicate the largest known RNA genomes. This protein complex is a fascinating example of the functional integration of RNA polymerase, capping, and proofreading activities. </div>
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<Abstract><AbstractText>In addition to members causing milder human infections, the Coronaviridae family includes potentially lethal zoonotic agents causing severe acute respiratory syndrome (SARS) and the recently emerged Middle East respiratory syndrome. The ∼30-kb positive-stranded RNA genome of coronaviruses encodes a replication/transcription machinery that is unusually complex and composed of 16 nonstructural proteins (nsps). SARS-CoV nsp12, the canonical RNA-dependent RNA polymerase (RdRp), exhibits poorly processive RNA synthesis in vitro, at odds with the efficient replication of a very large RNA genome in vivo. Here, we report that SARS-CoV nsp7 and nsp8 activate and confer processivity to the RNA-synthesizing activity of nsp12. Using biochemical assays and reverse genetics, the importance of conserved nsp7 and nsp8 residues was probed. Whereas several nsp7 mutations affected virus replication to a limited extent, the replacement of two nsp8 residues (P183 and R190) essential for interaction with nsp12 and a third (K58) critical for the interaction of the polymerase complex with RNA were all lethal to the virus. Without a loss of processivity, the nsp7/nsp8/nsp12 complex can associate with nsp14, a bifunctional enzyme bearing 3'-5' exoribonuclease and RNA cap N7-guanine methyltransferase activities involved in replication fidelity and 5'-RNA capping, respectively. The identification of this tripartite polymerase complex that in turn associates with the nsp14 proofreading enzyme sheds light on how coronaviruses assemble an RNA-synthesizing machinery to replicate the largest known RNA genomes. This protein complex is a fascinating example of the functional integration of RNA polymerase, capping, and proofreading activities. </AbstractText>
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One severe acute respiratory syndrome coronavirus protein complex integrates processive RNA polymerase and exonuclease activities.

One severe acute respiratory syndrome coronavirus protein complex integrates processive RNA polymerase and exonuclease activities.

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