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.