PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome
- PMID: 1825134
- DOI: 10.1038/349494a0
PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome
Abstract
The assembly of the spliceosome is an ATP-dependent process. The splicing factor PRP16 contains variations of several motifs that define the eIF-4A-like ATP-dependent RNA helicase family. The protein has now been purified and shown to exhibit RNA-dependent ATPase activity. PRP16 is required specifically for the second catalytic step of the splicing reaction in vitro. This function requires ATP binding and/or hydrolysis, which appears to be concomitant with release of the protein from the spliceosome. PRP16 may be the prototype for a set of splicing factors which use ATP to drive a cycle of conformational changes.
Comment in
-
RNA splicing. Alive with DEAD proteins.Nature. 1991 Feb 7;349(6309):463-4. doi: 10.1038/349463a0. Nature. 1991. PMID: 1825133 No abstract available.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases