PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome

Nature. 1991 Feb 7;349(6309):494-9. doi: 10.1038/349494a0.


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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases / genetics*
  • Adenosine Triphosphatases / metabolism
  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Cell-Free System
  • Genetic Complementation Test
  • In Vitro Techniques
  • Macromolecular Substances
  • Molecular Sequence Data
  • RNA Helicases
  • RNA Nucleotidyltransferases / metabolism
  • RNA Splicing*
  • Saccharomyces cerevisiae / genetics


  • Macromolecular Substances
  • Adenosine Triphosphate
  • RNA Nucleotidyltransferases
  • Adenosine Triphosphatases
  • RNA Helicases