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首页> 外文期刊>Biochemical and Biophysical Research Communications >Biochemical and functional studies on the regulation of the Saccharomyces cerevisiae AMPK homolog SNF1.
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Biochemical and functional studies on the regulation of the Saccharomyces cerevisiae AMPK homolog SNF1.

机译：生化和功能研究啤酒酵母AMPK同源SNF1的调节。

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摘要

AMP-activated protein kinase (AMPK) is a master metabolic regulator for controlling cellular energy homeostasis. Its homolog in yeast, SNF1, is activated in response to glucose depletion and other stresses. The catalytic (alpha) subunit of AMPK/SNF1, Snf1 in yeast, contains a protein Ser/Thr kinase domain (KD), an auto-inhibitory domain (AID), and a region that mediates interactions with the two regulatory (beta and gamma) subunits. Previous studies suggested that Snf1 contains an additional segment, a regulatory sequence (RS, corresponding to residues 392-518), which may also have an important role in regulating the activity of the enzyme. The crystal structure of the heterotrimer core of Saccharomyces cerevisiae SNF1 showed interactions between a part of the RS (residues 460-498) and the gamma subunit Snf4. Here we report biochemical and functional studies on the regulation of SNF1 by the RS. GST pulldown experiments demonstrate strong and direct interactions between residues 450-500 of the RS and the heterotrimer core, and single-site mutations in the RS-Snf4 interface can greatly reduce these interactions in vitro. On the other hand, functional studies appear to show only small effects of the RS-Snf4 interactions on the activity of SNF1 in vivo. This suggests that residues 450-500 may be constitutively associated with Snf4, and the remaining segments of the RS, as well as the AID, may be involved in regulating SNF1 activity.
机译：AMP激活的蛋白激酶（AMPK）是控制细胞能量稳态的主要代谢调节剂。它在酵母中的同系物SNF1响应葡萄糖耗尽和其他压力而被激活。酵母中AMPK / SNF1的催化亚基Snf1包含蛋白Ser / Thr激酶域（KD），自抑制域（AID）和介导与两个调节因子（beta和gamma）相互作用的区域）的子单元。先前的研究表明，Snf1包含一个额外的片段，一个调控序列（RS，对应于残基392-518），在调控酶的活性中也可能起重要作用。酿酒酵母SNF1的异三聚体核心的晶体结构显示部分RS（残基460-498）和γ亚基Snf4之间的相互作用。在这里，我们报告由RS调节SNF1的生化和功能研究。 GST下拉实验表明，RS的残基450-500与异三聚体核心之间发生了直接的强相互作用，而RS-Snf4界面中的单点突变可在体外大大减少这些相互作用。另一方面，功能研究似乎表明，RS-Snf4相互作用对SNF1体内活性的影响很小。这表明残基450-500可能与Snf4组成性结合，而RS的其余片段以及AID可能参与调节SNF1活性。

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