分子生物学文章求翻译NIPP1isaubiquitousnuclearproteinthatisrequiredforspliceosomeassembly.Wereportherethatthephos-phothreonine-bindingForkhead-associateddomainofNIPP1interactswiththecellcycle-regulatedproteinSer/Thr
分子生物学文章求翻译
NIPP1isaubiquitousnuclearproteinthatisrequired
forspliceosomeassembly.Wereportherethatthephos-
phothreonine-bindingForkhead-associateddomainof
NIPP1interactswiththecellcycle-regulatedprotein
Ser/ThrkinaseMELK(maternalembryonicleucinezip-
perkinase).TheNIPP1-MELKinteractionwascritically
dependentonthephosphorylatonofThr-478ofMELK
andwasincreasedinlysatesfrommitoticallyarrested
cells.RecombinantMELKwasapotentinhibitorofan
earlystepofspliceosomeassemblyinnuclearextracts.
Thissplicingdefectwasalsoseenwithakinase-dead
mutantbutwasabsentaftermutation(T478A)ofthe
NIPP1bindingsiteofMELK,indicatingamediatory
roleforNIPP1.OurdatasuggestthatMELKhasarolein
thecellcycle-regulatedcontrolofpre-mRNAsplicing.