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首页> 外文期刊>Molecular and Cellular Biology >The 70-kilodalton adenylyl cyclase-associated protein is not essential for interaction of Saccharomyces cerevisiae adenylyl cyclase with RAS proteins.
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The 70-kilodalton adenylyl cyclase-associated protein is not essential for interaction of Saccharomyces cerevisiae adenylyl cyclase with RAS proteins.

机译：70公斤的腺苷酸环化酶相关蛋白对于酿酒酵母腺苷酸环化酶与RAS蛋白的相互作用不是必需的。

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摘要

In the yeast Saccharomyces cerevisiae, adenylyl cyclase is regulated by RAS proteins. We show here that the yeast adenylyl cyclase forms at least two high-molecular-weight complexes, one with the RAS protein-dependent adenylyl cyclase activity and the other with the Mn(2+)-dependent activity, which are separable by their size difference. The 70-kDa adenylyl cyclase-associated protein (CAP) existed in the former complex but not in the latter. Missense mutations in conserved motifs of the leucine-rich repeats of the catalytic subunit of adenylyl cyclase abolished the RAS-dependent activity, which was accompanied by formation of a very high molecular weight complex having the Mn(2+)-dependent activity. Contrary to previous results, disruption of the gene encoding CAP did not alter the extent of RAS protein-dependent activation of adenylyl cyclase, while a concomitant decrease in the size of the RAS-responsive complex was observed. These results indicate that CAP is not essential for interaction of the yeast adenylyl cyclase with RAS proteins even though it is an inherent component of the RAS-responsive adenylyl cyclase complex.
机译：在酵母酿酒酵母中，腺苷酸环化酶受RAS蛋白的调节。我们在这里显示酵母腺苷酸环化酶形成至少两种高分子量复合物，一种具有RAS蛋白依赖性腺苷酸环化酶活性，而另一种具有Mn（2+）依赖性活性，这可以通过其大小差异来分离。 70 kDa的腺苷酸环化酶相关蛋白（CAP）存在于前一种复合物中，但不存在于后者中。腺苷酸环化酶催化亚基的富含亮氨酸重复序列的保守基序中的错义突变消除了RAS依赖性活性，伴随而来的是具有Mn（2+）依赖性活性的高分子量复合物的形成。与先前的结果相反，编码CAP的基因的破坏并没有改变RAS蛋白依赖性腺苷酸环化酶的活化程度，而同时观察到RAS反应复合物的大小随之减小。这些结果表明，CAP对于酵母腺苷酸环化酶与RAS蛋白的相互作用不是必需的，即使它是RAS应答性腺苷酸环化酶复合物的固有成分。

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