A protein kinase activity that phosphorylates the G-terminal domain (C
TD) of RNA polymerase II and is associated with the basal transcriptio
n-repair factor TFIIH (also called BTF2) resides with MO15, a cyclin-d
ependent protein kinase that was first found to be involved in cell cy
cle regulation. Using in vivo and in vitro repair assays, we show that
MO15 is important for nucleotide excision repair, most likely through
its association with TFIIH, thus providing an unexpected link among t
hree important cellular mechanisms.