Assembly of core helices and rapid tertiary folding of a small bacterial group I ribozyme
AUTOR(ES)
Rangan, Prashanth
FONTE
The National Academy of Sciences
RESUMO
Compact but non-native intermediates have been implicated in the hierarchical folding of several large RNAs, but there is little information on their structure. In this article, ribonuclease and hydroxyl radical cleavage protection assays showed that base pairing of core helices stabilize a compact state of a small group I ribozyme from Azoarcus pre-tRNAile. Base pairing of the ribozyme core requires 10-fold less Mg2+ than stable tertiary interactions, indicating that assembly of helices in the catalytic core represents a distinct phase that precedes the formation of native tertiary structure. Tertiary folding occurs in <100 ms at 37°C. Such rapid folding is unprecedented among group I ribozymes and illustrates the association between structural complexity and folding time. A 3D model of the Azoarcus ribozyme was constructed by identifying homologous sequence motifs in rRNA. The model reveals distinct structural features, such as a large interface between the P4–P6 and P3–P9 domains, that may explain the unusual stability of the Azoarcus ribozyme and the cooperativity of folding.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=149874Documentos Relacionados
- Folding of the group I intron ribozyme from the 26S rRNA gene of Candida albicans
- Visualizing the solvent-inaccessible core of a group II intron ribozyme
- Folding of group I introns from bacteriophage T4 involves internalization of the catalytic core.
- Modular engineering of a Group I intron ribozyme
- Bidirectional effectors of a group I intron ribozyme.