Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-9-22
pubmed:databankReference
pubmed:abstractText
NS53, the product of rotavirus gene 5, is an RNA-binding protein that contains a cysteine-rich region and is a component of early replication intermediates. To gain information about the structure of NS53 and its RNA, we determined the nucleotide sequence of gene 5 for the human viruses Wa (serotype 1) and DS1 (2) and the simian virus SA11 (3) (Patton strain) and compared them and their deduced amino acid sequences to those reported for the bovine viruses UK (6) and RF (6), SA11 (3) (Both strain), the human virus Rohivg803, and the group C porcine virus PRV. The results showed that gene 5 for human, simian, and bovine strains have lengths of 1564-1567, 1611, and 1579-1581 nucleotides (nt) and encode proteins of 486, 495, and 491 amino acids, respectively. Comparison of the protein sequences for NS53 among different serotypes showed that they are extremely divergent with many sharing amino acid homologies of only 36-38%. Even NS53 from viruses isolated from the same species possessed relatively poor homology, e.g., DS1 versus Wa was 68%. The first 150 amino acids of NS53 exhibited a greater degree of conservation than the rest of the protein. Near the amino terminus, NS53 contains three basic regions and a cysteine-rich domain, suggesting that this area is responsible for the RNA-binding activity of the protein. Present in the cysteine-rich domain of all group A and C viruses was the motif C-X2-C-X8-C-X2-C-X3-H-X-C-X2-C-X5-C. Although this motif may form one or two zinc fingers, the fact that it is highly conserved indicates that it plays a critical role in the function of protein. Comparison of the nucleotide sequences for gene 5 showed that the entire 5'-noncoding region and the first 24 nt of the NS53 ORF are conserved. RNA-folding predictions suggest that this region of the NS53 mRNA can interact with itself, producing a stem-loop structure similar to that found near the 5'-terminus of the NS35 mRNA. Thus, such structures may be common to all rotavirus mRNAs, perhaps functioning as signals for packaging of RNAs into replication intermediates or regulating mRNA translation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:volume
196
pubmed:geneSymbol
NS53
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
372-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8395125-Amino Acid Sequence, pubmed-meshheading:8395125-Animals, pubmed-meshheading:8395125-Base Sequence, pubmed-meshheading:8395125-Cell Line, pubmed-meshheading:8395125-Cysteine, pubmed-meshheading:8395125-DNA, Viral, pubmed-meshheading:8395125-Haplorhini, pubmed-meshheading:8395125-Humans, pubmed-meshheading:8395125-Hydrogen-Ion Concentration, pubmed-meshheading:8395125-Molecular Sequence Data, pubmed-meshheading:8395125-Nucleic Acid Conformation, pubmed-meshheading:8395125-Phylogeny, pubmed-meshheading:8395125-RNA, Viral, pubmed-meshheading:8395125-RNA-Binding Proteins, pubmed-meshheading:8395125-Rotavirus, pubmed-meshheading:8395125-Sequence Homology, Amino Acid, pubmed-meshheading:8395125-Sequence Homology, Nucleic Acid, pubmed-meshheading:8395125-Viral Nonstructural Proteins
pubmed:year
1993
pubmed:articleTitle
Comparative analysis of the rotavirus NS53 gene: conservation of basic and cysteine-rich regions in the protein and possible stem-loop structures in the RNA.
pubmed:affiliation
Department of Microbiology and Immunology, University of Miami School of Medicine, Florida 33101.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.