PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome.
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.
Schwer
B
B
Department of Biochemistry and Biophysics, University of California, San Francisco 94143.
Guthrie
C
C
D000251:Adenosine Triphosphatases / Q000235:genetics* / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D002474:Cell-Free System; D005816:Genetic Complementation Test; D066298:In Vitro Techniques; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D020365:RNA Helicases; D012316:RNA Nucleotidyltransferases / Q000378:metabolism; D012326:RNA Splicing; D012441:Saccharomyces cerevisiae / Q000235:genetics
D046911:Macromolecular Substances; D000255:Adenosine Triphosphate; D012316:RNA Nucleotidyltransferases; D000251:Adenosine Triphosphatases; D020365:RNA Helicases