Functional formation of domain V of the poliovirus noncoding region: significance of unpaired bases
| Autor: | A. Rowe, J. Burlison, Andrew J. Macadam, P.D. Minor |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Genetics
Mutation Base Sequence Poliovirus Revertant Molecular Sequence Data Temperature Biology medicine.disease_cause Cell Line Mice Virology Domain (ring theory) medicine Mutagenesis Site-Directed Animals Humans Nucleic Acid Conformation RNA Viral Temperature sensitive 5' Untranslated Regions Protein secondary structure |
| Zdroj: | Virology. 289(1) |
| ISSN: | 0042-6822 |
| Popis: | Previously we have shown that polioviruses with mutations that disrupt the predicted secondary structure of the 5′ noncoding region of domain V are temperature sensitive for growth. Non-temperature-sensitive revertant viruses had mutations that re-formed secondary structure by a direct back mutation of changes in the opposite strand. We mutated unpaired regions and selected revertants of viruses with single base deletions, where no obvious back mutation was available in order to gain information on secondary structure. Results indicated that conservation of length of a three base loop between two double-stranded stems was essential for a functional domain V to form. The requirement for the unpaired “hinge” base at 484 which is implicated in the attenuation of Sabin 2 was also confirmed. Results also underline the necessity for functional folding over local secondary structure stability. |
| Databáze: | OpenAIRE |
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