A conformational rearrangement in the spliceosome is dependent on PRP16 and ATP hydrolysis.

摘要: Abstract PRP16 is an RNA-dependent ATPase that required for the second catalytic step of pre-mRNA splicing. We have previously shown PRP16 protein binds stably to spliceosomes completed 5' splice site cleavage and lariat formation. then promotes 3' exon ligation in ATP-dependent fashion. now demonstrate can hydrolyse all nucleoside triphosphates corresponding deoxynucleotides; complementation shows same broad nucleotide specificity. These results link requirement 2 PRP16. Interestingly, we find a conformational change spliceosome which protection against oligo-directed RNase H cleavage. This structural rearrangement dependent on hydrolysis ATP, since ATP gamma S, competitive inhibitor activity, does not promote formation mRNA.