Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1992-9-10
pubmed:abstractText
The amino acid sequence of the poliovirus 2C protein contains two highly conserved stretches, GSPGTGKS136 and MDD177, which correspond to the consensus 'A' and 'B' motifs (GXXXXGKS/T and DD/E, respectively) found in nucleoside triphosphate-binding proteins. To assess the functional importance of these amino acid sequences, we changed conserved and non-conserved amino acids. The replacement of the non-conserved Thr133 residue with Ser or Ala did not markedly change the virus phenotype. Similarly, replacement of the non-conserved Pro131 residue by Ala did not abolish virus viability, but changes of this residue to Thr or Asn were not tolerated. No viable mutant could be isolated after transfection of cultured cells with transcripts mutated at the conserved Lys135, Ser136 or Asp177 residues. However, true revertants were selected from Arg135 and Ser135 mutants, from Glu177 and Gly177 mutants, and from Ala136 mutants. Thr136 mutants not only gave rise to true revertants, but also to two independent isolates of a suppressor mutant, Asn140----Tyr. All the lethal mutations resulted in severe inhibition of viral RNA synthesis in vivo, although no translational deficiency was detected in a cell-free system. This is the first direct evidence for the functional significance of the nucleoside triphosphate-binding pattern in the poliovirus 2C protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-1317
pubmed:author
pubmed:issnType
Print
pubmed:volume
73 ( Pt 8)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1977-86
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:1322957-Amino Acid Sequence, pubmed-meshheading:1322957-Base Sequence, pubmed-meshheading:1322957-Binding Sites, pubmed-meshheading:1322957-Carrier Proteins, pubmed-meshheading:1322957-Cloning, Molecular, pubmed-meshheading:1322957-Escherichia coli, pubmed-meshheading:1322957-HeLa Cells, pubmed-meshheading:1322957-Humans, pubmed-meshheading:1322957-Molecular Sequence Data, pubmed-meshheading:1322957-Mutagenesis, Site-Directed, pubmed-meshheading:1322957-Oligodeoxyribonucleotides, pubmed-meshheading:1322957-Phenotype, pubmed-meshheading:1322957-Plasmids, pubmed-meshheading:1322957-Poliovirus, pubmed-meshheading:1322957-RNA, Viral, pubmed-meshheading:1322957-Viral Nonstructural Proteins, pubmed-meshheading:1322957-Viral Plaque Assay, pubmed-meshheading:1322957-Viral Proteins, pubmed-meshheading:1322957-Virus Replication
pubmed:year
1992
pubmed:articleTitle
Analysis of the functional significance of amino acid residues in the putative NTP-binding pattern of the poliovirus 2C protein.
pubmed:affiliation
Unité de Virologie Moléculaire (CNRS UA 545), Institut Pasteur, Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't