A putative ATP binding protein influences the fidelity of branchpoint recognition in yeast splicing
| Autor: | Joseph R. Couto, Sean M. Burgess, Christine Guthrie |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Spliceosome
RNA Splicing Genes Fungal Molecular Sequence Data Saccharomyces cerevisiae Biology General Biochemistry Genetics and Molecular Biology Suppression Genetic Sequence Homology Nucleic Acid Consensus sequence Amino Acid Sequence Cloning Molecular Binding site Gene Library Genes Dominant Adenosine Triphosphatases Genetics Aspartic Acid Binding Sites Base Sequence Binding protein Intron Chromosome Mapping Cell biology A-site Mutation RNA splicing Tyrosine Sequence motif Plasmids |
| Zdroj: | Cell. 60:705-717 |
| ISSN: | 0092-8674 |
| DOI: | 10.1016/0092-8674(90)90086-t |
| Popis: | We previously described a dominant suppressor of the splicing defect conferred by an A----C intron branchpoint mutation in S. cerevisiae. Suppression occurs by increasing the frequency with which the mutant branchpoint is utilized. We have now cloned the genomic region encoding the prp16-1 suppressor function and have demonstrated that PRP16 is essential for viability. A 1071 amino acid open reading frame contains sequence motifs characteristic of an NTP binding fold and further similarities to a superfamily of proteins that includes members with demonstrated RNA-dependent ATPase activity. A single nucleotide change necessary to confer the prp16-1 suppressor phenotype results in a Tyr----Asp substitution near the "A site" consensus for NTP binding proteins. We propose that PRP16 is an excellent candidate for mediating one of the many ATP-requiring steps of spliceosome assembly and that accuracy of branchpoint recognition may be coupled to ATP binding and/or hydrolysis. |
| Databáze: | OpenAIRE |
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