SrasV1, PubMed, Checkpoint, bibRecord, 003032

The R protein of SARS-CoV: analyses of structure and function based on four complete genome sequences of isolates BJ01-BJ04.

Identifieur interne : 003032 ( PubMed/Checkpoint ); précédent : 003031; suivant : 003033

The R protein of SARS-CoV: analyses of structure and function based on four complete genome sequences of isolates BJ01-BJ04.

Auteurs : Zuyuan Xu [République populaire de Chine] ; Haiqing Zhang ; Xiangjun Tian ; Jia Ji ; Wei Li ; Yan Li ; Wei Tian ; Yujun Han ; Lili Wang ; Zizhang Zhang ; Jing Xu ; Wei Wei ; Jingui Zhu ; Haiyan Sun ; Xiaowei Zhang ; Jun Zhou ; Songgang Li ; Jun Wang ; Jian Wang ; Shengli Bi ; Huanming Yang

Source :

Genomics, proteomics & bioinformatics [ 1672-0229 ] ; 2003.

RBID : pubmed:15626345

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Base Composition, Base Sequence, Cluster Analysis, Computational Biology, Conserved Sequence (genetics), Evolution, Molecular, Gene Components, Genome, Viral, Molecular Sequence Data, Mutation (genetics), Phylogeny, Protein Structure, Tertiary, RNA Replicase (genetics), SARS Virus (genetics), Sequence Analysis, DNA.
MESH :
- chemical , genetics : RNA Replicase.
- genetics : Conserved Sequence, Mutation, SARS Virus.
- Amino Acid Sequence, Base Composition, Base Sequence, Cluster Analysis, Computational Biology, Evolution, Molecular, Gene Components, Genome, Viral, Molecular Sequence Data, Phylogeny, Protein Structure, Tertiary, Sequence Analysis, DNA.

Abstract

The R (replicase) protein is the uniquely defined non-structural protein (NSP) responsible for RNA replication, mutation rate or fidelity, regulation of transcription in coronaviruses and many other ssRNA viruses. Based on our complete genome sequences of four isolates (BJ01-BJ04) of SARS-CoV from Beijing, China, we analyzed the structure and predicted functions of the R protein in comparison with 13 other isolates of SARS-CoV and 6 other coronaviruses. The entire ORF (open-reading frame) encodes for two major enzyme activities, RNA-dependent RNA polymerase (RdRp) and proteinase activities. The R polyprotein undergoes a complex proteolytic process to produce 15 function-related peptides. A hydrophobic domain (HOD) and a hydrophilic domain (HID) are newly identified within NSP1. The substitution rate of the R protein is close to the average of the SARS-CoV genome. The functional domains in all NSPs of the R protein give different phylogenetic results that suggest their different mutation rate under selective pressure. Eleven highly conserved regions in RdRp and twelve cleavage sites by 3CLP (chymotrypsin-like protein) have been identified as potential drug targets. Findings suggest that it is possible to obtain information about the phylogeny of SARS-CoV, as well as potential tools for drug design, genotyping and diagnostics of SARS.

DOI: 10.1016/s1672-0229(03)01019-2
PubMed: 15626345

Affiliations:

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 002981
to stream PubMed, to step Curation: 002981

Links to Exploration step

pubmed:15626345

Le document en format XML

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<front><div type="abstract" xml:lang="en">The R (replicase) protein is the uniquely defined non-structural protein (NSP) responsible for RNA replication, mutation rate or fidelity, regulation of transcription in coronaviruses and many other ssRNA viruses. Based on our complete genome sequences of four isolates (BJ01-BJ04) of SARS-CoV from Beijing, China, we analyzed the structure and predicted functions of the R protein in comparison with 13 other isolates of SARS-CoV and 6 other coronaviruses. The entire ORF (open-reading frame) encodes for two major enzyme activities, RNA-dependent RNA polymerase (RdRp) and proteinase activities. The R polyprotein undergoes a complex proteolytic process to produce 15 function-related peptides. A hydrophobic domain (HOD) and a hydrophilic domain (HID) are newly identified within NSP1. The substitution rate of the R protein is close to the average of the SARS-CoV genome. The functional domains in all NSPs of the R protein give different phylogenetic results that suggest their different mutation rate under selective pressure. Eleven highly conserved regions in RdRp and twelve cleavage sites by 3CLP (chymotrypsin-like protein) have been identified as potential drug targets. Findings suggest that it is possible to obtain information about the phylogeny of SARS-CoV, as well as potential tools for drug design, genotyping and diagnostics of SARS.</div>
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<Abstract><AbstractText>The R (replicase) protein is the uniquely defined non-structural protein (NSP) responsible for RNA replication, mutation rate or fidelity, regulation of transcription in coronaviruses and many other ssRNA viruses. Based on our complete genome sequences of four isolates (BJ01-BJ04) of SARS-CoV from Beijing, China, we analyzed the structure and predicted functions of the R protein in comparison with 13 other isolates of SARS-CoV and 6 other coronaviruses. The entire ORF (open-reading frame) encodes for two major enzyme activities, RNA-dependent RNA polymerase (RdRp) and proteinase activities. The R polyprotein undergoes a complex proteolytic process to produce 15 function-related peptides. A hydrophobic domain (HOD) and a hydrophilic domain (HID) are newly identified within NSP1. The substitution rate of the R protein is close to the average of the SARS-CoV genome. The functional domains in all NSPs of the R protein give different phylogenetic results that suggest their different mutation rate under selective pressure. Eleven highly conserved regions in RdRp and twelve cleavage sites by 3CLP (chymotrypsin-like protein) have been identified as potential drug targets. Findings suggest that it is possible to obtain information about the phylogeny of SARS-CoV, as well as potential tools for drug design, genotyping and diagnostics of SARS.</AbstractText>
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The R protein of SARS-CoV: analyses of structure and function based on four complete genome sequences of isolates BJ01-BJ04.

The R protein of SARS-CoV: analyses of structure and function based on four complete genome sequences of isolates BJ01-BJ04.

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