Conversion of a DNA ligase into an RNA capping enzyme.
AUTOR(ES)
Doherty, A J
RESUMO
In eukaryotes, newly synthesised mRNA is 'capped' by the addition of GMP to the 5" end by RNA capping enzymes. Recent structural studies have shown that RNA capping enzymes and DNA ligases have similar protein folds, suggesting a conserved catalytic mechanism. To explore these similarities we have produced a chimeric enzyme comprising the N-terminal domain 1 of a DNA ligase fused to the C-terminal domain 2 of a mRNA capping enzyme. This report shows that this hybrid enzyme retains adenylation activity, characteristic of DNA ligases but, remarkably, the chimera has ATP-dependent mRNA capping activity. This is the first observation of ATP-dependent RNA capping. These results suggest that nucleotidyltransferases may have evolved from a common ancestral gene.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=148557Documentos Relacionados
- Mutational analysis of yeast mRNA capping enzyme.
- Isolation and characterization of a human cDNA for mRNA 5'-capping enzyme.
- A Saccharomyces cerevisiae RNA 5'-triphosphatase related to mRNA capping enzyme.
- Accelerated mRNA decay in conditional mutants of yeast mRNA capping enzyme.
- Mutational analysis of the RNA triphosphatase component of vaccinia virus mRNA capping enzyme.
