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Securin is a cytoplasmic protein that binds to separase, an enzyme that degrades cohesin. when separase is bound to securin, separase is inactive. when separase is released, it immediately becomes active. securin and separase remain attached to each other as long as securin is phosphorylated. based on the role of securin, it must become dephosphorylated just prior to

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W0lf93
Cohesin holds the sister chromatids together after DNA replication, and removal of cohesin leads to separation of the sister chromatids. Securin is part of the metaphase-anaphase transition and anaphase onset and is required to ensure that separase is folded properly. Since Securin must be degraded for anaphase and the subsequence degradation of cohesin to occur, it must be dephosphorylated just prior to anaphase.

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