作业帮分子生物学文章求翻译NIPP1 is a ubiquitous nuclear protein that is requiredfor spliceosome assembly. We report here that the phos-phothreonine-binding Forkhead-associated domain ofNIPP1 interacts with the cell cycle-regulated proteinSer/Thr
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分子生物学文章求翻译NIPP1 is a ubiquitous nuclear protein that is requiredfor spliceosome assembly. We report here that the phos-phothreonine-binding Forkhead-associated domain ofNIPP1 interacts with the cell cycle-regulated proteinSer/Thr
分子生物学文章求翻译
NIPP1 is a ubiquitous nuclear protein that is required
for spliceosome assembly. We report here that the phos-
phothreonine-binding Forkhead-associated domain of
NIPP1 interacts with the cell cycle-regulated protein
Ser/Thr kinase MELK (maternal embryonic leucine zip-
per kinase). The NIPP1-MELK interaction was critically
dependent on the phosphorylaton of Thr-478 of MELK
and was increased in lysates from mitotically arrested
cells. Recombinant MELK was a potent inhibitor of an
early step of spliceosome assembly in nuclear extracts.
This splicing defect was also seen with a kinase-dead
mutant but was absent after mutation (T478A) of the
NIPP1 binding site of MELK, indicating a mediatory
role for NIPP1. Our data suggest that MELK has a role in
the cell cycle-regulated control of pre-mRNA splicing.
分子生物学文章求翻译NIPP1 is a ubiquitous nuclear protein that is requiredfor spliceosome assembly. We report here that the phos-phothreonine-binding Forkhead-associated domain ofNIPP1 interacts with the cell cycle-regulated proteinSer/Thr
NIPP1是一种普遍存在于细胞核中的蛋白,它在剪接体的装配中必须是的.在这里,我们报道NIPP1中与磷酸化苏氨酸结合的forkhead相关结构域和细胞周期调控蛋白——Ser/Thr激酶MELK之间的相互作用.NIPP1与MELK之间的作用严格依赖于MELK第478位苏氨酸的磷酸化,并且,这种相互作用在有丝分裂被阻断的细胞的裂解液中有所增强.在细胞核提取液中,MELK是剪接复合体早期装配过程中的一个潜在的抑制剂.这种剪接不能的现象也可见于激酶致死型的突变体中,然而,当MELK中与NIPP1的结合位点突变（T478A）之后却不会导致剪接的异常,这提示MELK对NIPP1有调节功能.我们的资料显示MELK通过对pre-mRNA剪接的控制来参与细胞周期的调控.
翻译得比较粗糙,大体就这意思了.