The 3a accessory protein of SARS coronavirus specifically interacts with the 5'UTR of its genomic RNA, Using a unique 75 amino acid interaction domain.
Identifieur interne : 001E25 ( PubMed/Corpus ); précédent : 001E24; suivant : 001E26The 3a accessory protein of SARS coronavirus specifically interacts with the 5'UTR of its genomic RNA, Using a unique 75 amino acid interaction domain.
Auteurs : Kulbhushan Sharma ; Milan Surjit ; Namita Satija ; Boping Liu ; Vincent T K. Chow ; Sunil K. LalSource :
- Biochemistry [ 0006-2960 ] ; 2007.
English descriptors
- KwdEn :
- Amino Acid Motifs, Amino Acid Sequence, Electrophoretic Mobility Shift Assay, Gene Deletion, Gene Expression Regulation, Viral, Genome, Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (genetics), Nucleocapsid Proteins (metabolism), Protein Binding, RNA, Viral (chemistry), RNA, Viral (metabolism), RNA-Binding Proteins (chemistry), RNA-Binding Proteins (genetics), RNA-Binding Proteins (metabolism), SARS Virus (chemistry), SARS Virus (genetics), Saccharomyces cerevisiae (chemistry), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Two-Hybrid System Techniques, Ultraviolet Rays, Untranslated Regions (chemistry), Untranslated Regions (genetics), Untranslated Regions (metabolism).
- MESH :
- chemical , chemistry : Nucleocapsid Proteins, RNA, Viral, RNA-Binding Proteins, Untranslated Regions.
- chemical , genetics : Nucleocapsid Proteins, RNA-Binding Proteins, Untranslated Regions.
- chemical , metabolism : Nucleocapsid Proteins, RNA, Viral, RNA-Binding Proteins, Untranslated Regions.
- chemistry : SARS Virus, Saccharomyces cerevisiae.
- genetics : SARS Virus, Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Amino Acid Motifs, Amino Acid Sequence, Electrophoretic Mobility Shift Assay, Gene Deletion, Gene Expression Regulation, Viral, Genome, Protein Binding, Two-Hybrid System Techniques, Ultraviolet Rays.
Abstract
More than four years have passed since the outbreak of the severe acute respiratory syndrome (SARS) epidemic, and still very little is known about the molecular biology and pathogenesis of this deadly virus. Among the accessory proteins of the SARS coronavirus (SARS-CoV), the 3a protein has been shown to interact with the spike, envelope, and membrane glycoprotein and has recently been established to be a structural component of capsid. Recent studies suggest that the 3a protein may function as an ion channel and may promote virus release. In order to further characterize the functional properties of this protein, we initiated studies to check its RNA binding activity. Using the yeast three-hybrid system, electrophoretic mobility shift assay (EMSA), and ultraviolet (UV) cross-linking techniques, we have shown that the 3a protein is capable of binding specifically to the 5' untranslated region (5'UTR) of the SARS virus genomic RNA. Further, we have mapped the interaction domain of the 3a protein responsible for this RNA-protein interaction using a series of deletion mutants and defined it to the central 75 amino acid region. This RNA binding motif of 3a does not share homology with any other known RNA binding protein and may have an important role in viral capsid assembly and pathogenesis.
DOI: 10.1021/bi062057p
PubMed: 17488094
Links to Exploration step
pubmed:17488094Le document en format XML
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Chow</name></author><author><name sortKey="Lal, Sunil K" sort="Lal, Sunil K" uniqKey="Lal S" first="Sunil K" last="Lal">Sunil K. Lal</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17488094</idno><idno type="pmid">17488094</idno><idno type="doi">10.1021/bi062057p</idno><idno type="wicri:Area/PubMed/Corpus">001E25</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001E25</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The 3a accessory protein of SARS coronavirus specifically interacts with the 5'UTR of its genomic RNA, Using a unique 75 amino acid interaction domain.</title><author><name sortKey="Sharma, Kulbhushan" sort="Sharma, Kulbhushan" uniqKey="Sharma K" first="Kulbhushan" last="Sharma">Kulbhushan Sharma</name><affiliation><nlm:affiliation>Virology Group, International Centre for Genetic Engineering & Biotechnology, Aruna Asaf Ali Road, New Delhi 110067, India.</nlm:affiliation></affiliation></author><author><name sortKey="Surjit, Milan" sort="Surjit, Milan" uniqKey="Surjit M" first="Milan" last="Surjit">Milan Surjit</name></author><author><name sortKey="Satija, Namita" sort="Satija, Namita" uniqKey="Satija N" first="Namita" last="Satija">Namita Satija</name></author><author><name sortKey="Liu, Boping" sort="Liu, Boping" uniqKey="Liu B" first="Boping" last="Liu">Boping Liu</name></author><author><name sortKey="Chow, Vincent T K" sort="Chow, Vincent T K" uniqKey="Chow V" first="Vincent T K" last="Chow">Vincent T K. Chow</name></author><author><name sortKey="Lal, Sunil K" sort="Lal, Sunil K" uniqKey="Lal S" first="Sunil K" last="Lal">Sunil K. Lal</name></author></analytic><series><title level="j">Biochemistry</title><idno type="ISSN">0006-2960</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Electrophoretic Mobility Shift Assay</term><term>Gene Deletion</term><term>Gene Expression Regulation, Viral</term><term>Genome</term><term>Nucleocapsid Proteins (chemistry)</term><term>Nucleocapsid Proteins (genetics)</term><term>Nucleocapsid Proteins (metabolism)</term><term>Protein Binding</term><term>RNA, Viral (chemistry)</term><term>RNA, Viral (metabolism)</term><term>RNA-Binding Proteins (chemistry)</term><term>RNA-Binding Proteins (genetics)</term><term>RNA-Binding Proteins (metabolism)</term><term>SARS Virus (chemistry)</term><term>SARS Virus (genetics)</term><term>Saccharomyces cerevisiae (chemistry)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Two-Hybrid System Techniques</term><term>Ultraviolet Rays</term><term>Untranslated Regions (chemistry)</term><term>Untranslated Regions (genetics)</term><term>Untranslated Regions (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nucleocapsid Proteins</term><term>RNA, Viral</term><term>RNA-Binding Proteins</term><term>Untranslated Regions</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Nucleocapsid Proteins</term><term>RNA-Binding Proteins</term><term>Untranslated Regions</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Nucleocapsid Proteins</term><term>RNA, Viral</term><term>RNA-Binding Proteins</term><term>Untranslated Regions</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Electrophoretic Mobility Shift Assay</term><term>Gene Deletion</term><term>Gene Expression Regulation, Viral</term><term>Genome</term><term>Protein Binding</term><term>Two-Hybrid System Techniques</term><term>Ultraviolet Rays</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">More than four years have passed since the outbreak of the severe acute respiratory syndrome (SARS) epidemic, and still very little is known about the molecular biology and pathogenesis of this deadly virus. Among the accessory proteins of the SARS coronavirus (SARS-CoV), the 3a protein has been shown to interact with the spike, envelope, and membrane glycoprotein and has recently been established to be a structural component of capsid. Recent studies suggest that the 3a protein may function as an ion channel and may promote virus release. In order to further characterize the functional properties of this protein, we initiated studies to check its RNA binding activity. Using the yeast three-hybrid system, electrophoretic mobility shift assay (EMSA), and ultraviolet (UV) cross-linking techniques, we have shown that the 3a protein is capable of binding specifically to the 5' untranslated region (5'UTR) of the SARS virus genomic RNA. Further, we have mapped the interaction domain of the 3a protein responsible for this RNA-protein interaction using a series of deletion mutants and defined it to the central 75 amino acid region. This RNA binding motif of 3a does not share homology with any other known RNA binding protein and may have an important role in viral capsid assembly and pathogenesis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17488094</PMID><DateCompleted><Year>2007</Year><Month>07</Month><Day>05</Day></DateCompleted><DateRevised><Year>2007</Year><Month>05</Month><Day>29</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-2960</ISSN><JournalIssue CitedMedium="Print"><Volume>46</Volume><Issue>22</Issue><PubDate><Year>2007</Year><Month>Jun</Month><Day>05</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>The 3a accessory protein of SARS coronavirus specifically interacts with the 5'UTR of its genomic RNA, Using a unique 75 amino acid interaction domain.</ArticleTitle><Pagination><MedlinePgn>6488-99</MedlinePgn></Pagination><Abstract><AbstractText>More than four years have passed since the outbreak of the severe acute respiratory syndrome (SARS) epidemic, and still very little is known about the molecular biology and pathogenesis of this deadly virus. Among the accessory proteins of the SARS coronavirus (SARS-CoV), the 3a protein has been shown to interact with the spike, envelope, and membrane glycoprotein and has recently been established to be a structural component of capsid. Recent studies suggest that the 3a protein may function as an ion channel and may promote virus release. In order to further characterize the functional properties of this protein, we initiated studies to check its RNA binding activity. Using the yeast three-hybrid system, electrophoretic mobility shift assay (EMSA), and ultraviolet (UV) cross-linking techniques, we have shown that the 3a protein is capable of binding specifically to the 5' untranslated region (5'UTR) of the SARS virus genomic RNA. Further, we have mapped the interaction domain of the 3a protein responsible for this RNA-protein interaction using a series of deletion mutants and defined it to the central 75 amino acid region. This RNA binding motif of 3a does not share homology with any other known RNA binding protein and may have an important role in viral capsid assembly and pathogenesis.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sharma</LastName><ForeName>Kulbhushan</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Virology Group, International Centre for Genetic Engineering & Biotechnology, Aruna Asaf Ali Road, New Delhi 110067, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Surjit</LastName><ForeName>Milan</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Satija</LastName><ForeName>Namita</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Boping</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Chow</LastName><ForeName>Vincent T K</ForeName><Initials>VT</Initials></Author><Author ValidYN="Y"><LastName>Lal</LastName><ForeName>Sunil 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MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012367" MajorTopicYN="N">RNA, Viral</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016601" MajorTopicYN="N">RNA-Binding Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020798" MajorTopicYN="N">Two-Hybrid System Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014466" MajorTopicYN="N">Ultraviolet Rays</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020506" MajorTopicYN="N">Untranslated Regions</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate 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