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首页> 外文期刊>Cell cycle >Cyclin A degradation employs preferentially used lysines and a cyclin box function other than Cdk1 binding.
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Cyclin A degradation employs preferentially used lysines and a cyclin box function other than Cdk1 binding.

机译：细胞周期蛋白A降解采用优先使用的赖氨酸和除Cdk1结合以外的细胞周期蛋白盒功能。

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Cyclin A is targeted for mitotic destruction by the anaphase promoting complex/cyclosome (APC/C) and degradation proceeds even when proteolysis of other APC/C substrates are blocked by the spindle assembly checkpoint. Instead of a simple destruction box, a complex N-terminal destruction signal has been implicated in Cyclin A. We show here that Drosophila Cyclin A destruction employs both N- and C-terminal residues, which emphasize that a synergistic action by different parts of the protein facilitates recognition and degradation. The first KEN box, first D-box and an aspartic acid at position 70 are required at the N-terminus and they make additive contributions when the spindle checkpoint is active. From the C-terminal region, the cyclin box contributes. Single point mutations in these four elements abolish mitotic destruction. Additionally, eight lysines in the neighborhood of the N-terminal signals, which could serve as potential ubiquitin acceptor sites, are preferentially used for proteolysis. Mutations in these lysines and the N-terminal signals cause mitotic stability. However, mutating the lysines alone, only delays mitotic progression. Thus, presumably, lysines elsewhere in the protein are used when the preferred ones are absent and this requires the N-terminal signals. Furthermore, our results suggest that some function of the cyclin box other than Cdk1 binding promotes spindle checkpoint-independent recognition of Cyclin A by the APC/C.
机译：细胞周期蛋白A的目标是通过后期促进复合物/环体（APC / C）破坏有丝分裂，即使其他APC / C底物的蛋白水解被纺锤体组装检查点阻止，降解仍会继续进行。 Cyclin A牵涉到一个复杂的N端破坏信号，而不是一个简单的破坏盒。我们在这里表明，果蝇Cyclin A破坏同时利用了N和C端残基，这强调了不同部位的协同作用。蛋白质有助于识别和降解。 N端需要在位置70处有第一个KEN盒，第一个D盒和天冬氨酸，当激活主轴检查点时，它们会产生累加作用。在C末端区域，细胞周期蛋白框起作用。这四个要素中的单点突变消除了有丝分裂破坏。另外，在N-末端信号附近的八个赖氨酸可被用作潜在的泛素受体位点，被优先用于蛋白水解。这些赖氨酸和N端信号的突变会导致有丝分裂稳定性。但是，仅突变赖氨酸只会延迟有丝分裂的进程。因此，据推测，当缺少优选的蛋白质时，在蛋白质的其他地方使用了赖氨酸，这需要N端信号。此外，我们的结果表明，除了Cdk1结合外，细胞周期蛋白盒的某些功能还可以促进APC / C对细胞周期蛋白A的纺锤体检查点独立识别。

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