The structure of a rigorously conserved RNA element within the SARS virus genome.
Identifieur interne : 000C97 ( Ncbi/Merge ); précédent : 000C96; suivant : 000C98The structure of a rigorously conserved RNA element within the SARS virus genome.
Auteurs : Michael P. Robertson [États-Unis] ; Haller Igel ; Robert Baertsch ; David Haussler ; Manuel Ares ; William G. ScottSource :
- PLoS biology [ 1545-7885 ] ; 2005.
Descripteurs français
- KwdFr :
- MESH :
- génétique : Virus du SRAS.
- métabolisme : ARN messager.
- ARN viral, Conformation d'acide nucléique, Cristallographie aux rayons X, Données de séquences moléculaires, Génome viral, Humains, Mutation, Purines, Sites de fixation, Séquence conservée.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Purines, RNA, Viral.
- chemical , metabolism : RNA, Messenger.
- genetics : SARS Virus.
- Binding Sites, Conserved Sequence, Crystallography, X-Ray, Genome, Viral, Humans, Molecular Sequence Data, Mutation, Nucleic Acid Conformation.
Abstract
We have solved the three-dimensional crystal structure of the stem-loop II motif (s2m) RNA element of the SARS virus genome to 2.7-A resolution. SARS and related coronaviruses and astroviruses all possess a motif at the 3' end of their RNA genomes, called the s2m, whose pathogenic importance is inferred from its rigorous sequence conservation in an otherwise rapidly mutable RNA genome. We find that this extreme conservation is clearly explained by the requirement to form a highly structured RNA whose unique tertiary structure includes a sharp 90 degrees kink of the helix axis and several novel longer-range tertiary interactions. The tertiary base interactions create a tunnel that runs perpendicular to the main helical axis whose interior is negatively charged and binds two magnesium ions. These unusual features likely form interaction surfaces with conserved host cell components or other reactive sites required for virus function. Based on its conservation in viral pathogen genomes and its absence in the human genome, we suggest that these unusual structural features in the s2m RNA element are attractive targets for the design of anti-viral therapeutic agents. Structural genomics has sought to deduce protein function based on three-dimensional homology. Here we have extended this approach to RNA by proposing potential functions for a rigorously conserved set of RNA tertiary structural interactions that occur within the SARS RNA genome itself. Based on tertiary structural comparisons, we propose the s2m RNA binds one or more proteins possessing an oligomer-binding-like fold, and we suggest a possible mechanism for SARS viral RNA hijacking of host protein synthesis, both based upon observed s2m RNA macromolecular mimicry of a relevant ribosomal RNA fold.
DOI: 10.1371/journal.pbio.0030005
PubMed: 15630477
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Scott</name></author></analytic><series><title level="j">PLoS biology</title><idno type="eISSN">1545-7885</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites</term><term>Conserved Sequence</term><term>Crystallography, X-Ray</term><term>Genome, Viral</term><term>Humans</term><term>Molecular Sequence Data</term><term>Mutation</term><term>Nucleic Acid Conformation</term><term>Purines (chemistry)</term><term>RNA, Messenger (metabolism)</term><term>RNA, Viral (chemistry)</term><term>SARS Virus (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN messager (métabolisme)</term><term>ARN viral ()</term><term>Conformation d'acide nucléique</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Génome viral</term><term>Humains</term><term>Mutation</term><term>Purines ()</term><term>Sites de fixation</term><term>Séquence conservée</term><term>Virus du SRAS (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Purines</term><term>RNA, Viral</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>RNA, Messenger</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ARN messager</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Conserved Sequence</term><term>Crystallography, X-Ray</term><term>Genome, Viral</term><term>Humans</term><term>Molecular Sequence Data</term><term>Mutation</term><term>Nucleic Acid Conformation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>ARN viral</term><term>Conformation d'acide nucléique</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Génome viral</term><term>Humains</term><term>Mutation</term><term>Purines</term><term>Sites de fixation</term><term>Séquence conservée</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We have solved the three-dimensional crystal structure of the stem-loop II motif (s2m) RNA element of the SARS virus genome to 2.7-A resolution. SARS and related coronaviruses and astroviruses all possess a motif at the 3' end of their RNA genomes, called the s2m, whose pathogenic importance is inferred from its rigorous sequence conservation in an otherwise rapidly mutable RNA genome. We find that this extreme conservation is clearly explained by the requirement to form a highly structured RNA whose unique tertiary structure includes a sharp 90 degrees kink of the helix axis and several novel longer-range tertiary interactions. The tertiary base interactions create a tunnel that runs perpendicular to the main helical axis whose interior is negatively charged and binds two magnesium ions. These unusual features likely form interaction surfaces with conserved host cell components or other reactive sites required for virus function. Based on its conservation in viral pathogen genomes and its absence in the human genome, we suggest that these unusual structural features in the s2m RNA element are attractive targets for the design of anti-viral therapeutic agents. Structural genomics has sought to deduce protein function based on three-dimensional homology. Here we have extended this approach to RNA by proposing potential functions for a rigorously conserved set of RNA tertiary structural interactions that occur within the SARS RNA genome itself. Based on tertiary structural comparisons, we propose the s2m RNA binds one or more proteins possessing an oligomer-binding-like fold, and we suggest a possible mechanism for SARS viral RNA hijacking of host protein synthesis, both based upon observed s2m RNA macromolecular mimicry of a relevant ribosomal RNA fold.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15630477</PMID><DateCompleted><Year>2006</Year><Month>05</Month><Day>05</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1545-7885</ISSN><JournalIssue CitedMedium="Internet"><Volume>3</Volume><Issue>1</Issue><PubDate><Year>2005</Year><Month>Jan</Month></PubDate></JournalIssue><Title>PLoS biology</Title><ISOAbbreviation>PLoS Biol.</ISOAbbreviation></Journal><ArticleTitle>The structure of a rigorously conserved RNA element within the SARS virus genome.</ArticleTitle><Pagination><MedlinePgn>e5</MedlinePgn></Pagination><Abstract><AbstractText>We have solved the three-dimensional crystal structure of the stem-loop II motif (s2m) RNA element of the SARS virus genome to 2.7-A resolution. SARS and related coronaviruses and astroviruses all possess a motif at the 3' end of their RNA genomes, called the s2m, whose pathogenic importance is inferred from its rigorous sequence conservation in an otherwise rapidly mutable RNA genome. We find that this extreme conservation is clearly explained by the requirement to form a highly structured RNA whose unique tertiary structure includes a sharp 90 degrees kink of the helix axis and several novel longer-range tertiary interactions. The tertiary base interactions create a tunnel that runs perpendicular to the main helical axis whose interior is negatively charged and binds two magnesium ions. These unusual features likely form interaction surfaces with conserved host cell components or other reactive sites required for virus function. Based on its conservation in viral pathogen genomes and its absence in the human genome, we suggest that these unusual structural features in the s2m RNA element are attractive targets for the design of anti-viral therapeutic agents. Structural genomics has sought to deduce protein function based on three-dimensional homology. Here we have extended this approach to RNA by proposing potential functions for a rigorously conserved set of RNA tertiary structural interactions that occur within the SARS RNA genome itself. Based on tertiary structural comparisons, we propose the s2m RNA binds one or more proteins possessing an oligomer-binding-like fold, and we suggest a possible mechanism for SARS viral RNA hijacking of host protein synthesis, both based upon observed s2m RNA macromolecular mimicry of a relevant ribosomal RNA fold.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Robertson</LastName><ForeName>Michael P</ForeName><Initials>MP</Initials><AffiliationInfo><Affiliation>The Center for the Molecular Biology of RNA, University of California, Santa Cruz, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Igel</LastName><ForeName>Haller</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Baertsch</LastName><ForeName>Robert</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Haussler</LastName><ForeName>David</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Ares</LastName><ForeName>Manuel</ForeName><Initials>M</Initials><Suffix>Jr</Suffix></Author><Author ValidYN="Y"><LastName>Scott</LastName><ForeName>William G</ForeName><Initials>WG</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>1D7Q</AccessionNumber><AccessionNumber>1HR0</AccessionNumber><AccessionNumber>1J5E</AccessionNumber><AccessionNumber>1QZ8</AccessionNumber><AccessionNumber>1UW7</AccessionNumber><AccessionNumber>1XJR</AccessionNumber></AccessionNumberList></DataBank></DataBankList><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM087721</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType 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sortKey="Scott, William G" sort="Scott, William G" uniqKey="Scott W" first="William G" last="Scott">William G. Scott</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Robertson, Michael P" sort="Robertson, Michael P" uniqKey="Robertson M" first="Michael P" last="Robertson">Michael P. Robertson</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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