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The emerging regulatory potential of SCFMet30 -mediated polyubiquitination and proteolysis of the Met4 transcriptional activator

机译：SCFMet30介导的多泛素化和Met4转录激活子的蛋白水解的调节潜力

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The yeast SCFMet30 ubiquitin ligase plays a critical role in cell division by regulating the Met4 transcriptional activator of genes that control the uptake and assimilation of sulfur into methionine and S-adenosyl-methionine. The initial view on how SCFMet30 performs its function has been driven by the assumption that SCFMet30 acts exclusively as Met4 inhibitor when high levels of methionine drive an accumulation of cysteine. We revisit this model in light of the growing evidence that SCFMet30 can also activate Met4. The notion that Met4 can be inhibited or activated depending on the sulfur metabolite context is not new, but for the first time both aspects have been linked to SCFMet30, creating an interesting regulatory paradigm in which polyubiquitination and proteolysis of a single transcriptional activator can play different roles depending on context. We discuss the emerging molecular basis and the implications of this new regulatory phenomenon.
机译：酵母SCF Met30 泛素连接酶通过调节控制Met4转录激活因子的基因在细胞分裂中起关键作用，该基因控制硫的吸收和同化成蛋氨酸和S-腺苷甲硫氨酸。关于SCF Met30 如何执行其功能的最初观点是基于这样的假设，即当高水平的蛋氨酸驱动半胱氨酸积累时，SCF Met30 专门充当Met4抑制剂。鉴于越来越多的证据表明SCF Met30 也可以激活Met4，我们将重新研究该模型。可以根据硫代谢物的情况抑制或激活Met4的观念并不新鲜，但是这两个方面都首次与SCF Met30 相关联，从而创造了一种有趣的调控范式，其中多泛素化和蛋白水解单个转录激活因子的表达可以根据环境发挥不同的作用。我们讨论了新兴的分子基础和这种新的监管现象的含义。

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