Interaction of Escherichia coli DbpA with 23S rRNA in different functional states of the enzyme
AUTOR(ES)
Karginov, Fedor V.
FONTE
Oxford University Press
RESUMO
DExD/H proteins catalyze structural rearrangements in RNA by coupling ATP hydrolysis to the destabilization of RNA helices or RNP complexes. The Escherichia coli DExD/H protein DbpA specifically recognizes a region within the catalytic core of 23S rRNA. To better characterize the interaction of DbpA with this region and to identify changes in the complex between different nucleotide-bound states of the enzyme, RNase T1, RNase T2, kethoxal and DMS footprinting of DbpA on a 172 nt fragment of 23S rRNA were performed. A number of protections identified in helices 90 and 92 were consistent with biochemical experiments measuring the RNA binding and ATPase activity of DbpA with truncated RNAs. When DbpA was bound with AMPPNP, but not ADP, several additional footprints were detected in helix 93 and the single-stranded region 5′ of helix 90, suggesting binding of the helicase domains of DbpA at these sites. These results propose that DbpA can act at multiple sites and hint at the targets of its biological activity on rRNA.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=434445Documentos Relacionados
- Escherichia coli DbpA is an RNA helicase that requires hairpin 92 of 23S rRNA
- The "DEAD box" protein DbpA interacts specifically with the peptidyltransferase center in 23S rRNA.
- DbpA: a DEAD box protein specifically activated by 23s rRNA.
- A functional peptide encoded in the Escherichia coli 23S rRNA.
- Ordered processing of Escherichia coli 23S rRNA in vitro.