The catalytic core of RNase P.
AUTOR(ES)
Green, C J
RESUMO
A deletion mutant of the catalytic RNA component of Escherichia coli RNase P missing residues 87-241 retains the ability to interact with the protein component to form a functional catalyst. The deletion of this phylogenetically conserved region significantly increases the Km, indicating that the deleted structures may be important for binding to the precursor tRNA substrate but not for the cleavage reaction. Under some reaction conditions, this RNase P deletion mutant can become a relatively non-specific nuclease, indicating that this RNA's catalytic center may be more exposed. The catalytic core of the RNase P is formed by less than one third of the 377 residues of the RNase P RNA.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=145812Documentos Relacionados
- A novel tertiary interaction in M1 RNA, the catalytic subunit of Escherichia coli RNase P.
- Artificial self-cleaving molecules consisting of a tRNA precursor and the catalytic RNA of RNase P.
- Heterologous enzyme function in Escherichia coli and the selection of genes encoding the catalytic RNA subunit of RNase P.
- Product release is a rate-limiting step during cleavage by the catalytic RNA subunit of Escherichia coli RNase P.
- Different cleavage sites are aligned differently in the active site of M1 RNA, the catalytic subunit of Escherichia coli RNase P.