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首页> 外文期刊>Molecular and Cellular Biology >Properties and Possible Functions of the Adenylate Cyclase in Plasma Membranes of Saccharomyces cerevisiae
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Properties and Possible Functions of the Adenylate Cyclase in Plasma Membranes of Saccharomyces cerevisiae

机译：酿酒酵母血浆膜中腺苷酸环化酶的性质和可能的功能

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We have examined the possible role of adenosine 3′,5′-phosphate (cAMP) in functions associated with the plasma membranes of Saccharomyces cerevisiae. Purified membranes from this source contained an adenylate cyclase which was insensitive to activation by fluoride or guanine nucleotides, only weakly responsive to changes of carbon source in the growth medium, and strongly stimulated by vanadate. They also contained at least two classes of receptor proteins for guanine nucleotides (as measured by binding of labeled 5′-guanylyl methylene diphosphate) with apparent dissociation constants equal to 1.0 × 10?7 and 3 × 10?6 M, a protein kinase capable of phosphorylating added histones, the activity of which was stimulated by cAMP, and cAMP receptors that may function as regulatory subunits for this kinase. Membrane proteins were also susceptible to phosphorylation by endogenous kinase(s), with polypeptides of apparent molecular weights equal to 160 × 103, 135 × 103, 114 × 103, and 58 × 103 as the major targets. Of these, the 114,000-molecular-weight polypeptide was probably identical to the proton-translocating ATPase of the membranes. However, the cAMP-dependent protein kinase did not appear to be involved in these reactions. Intact (rho+ or rho0) cells responded to dissipation of the proton electrochemical gradient across their plasma membranes by rapid and transient changes in their intracellular level of cAMP, as suggested earlier (J. M. Trevillyan and M. L. Pall, J. Bacteriol., >138:397-403, 1979). Thus, although yeast plasma membranes contain all the essential components of a stimulus-responsive adenylate cyclase system, the precise nature of the coupling device and the targets involved remain to be established.
机译：我们研究了腺苷3'，5'-磷酸（cAMP）在与酿酒酵母细胞膜相关功能中的可能作用。从该来源纯化的膜含有对活化不敏感的腺苷酸环化酶。通过氟化物或鸟嘌呤核苷酸，仅对生长培养基中碳源的变化反应较弱，而受钒酸盐强烈刺激。它们还包含至少两类鸟嘌呤核苷酸的受体蛋白（通过标记的5'-鸟苷基亚甲基二磷酸的结合测量），表观解离常数等于1.0×10 和3×10 < sup>？6 M，一种能够磷酸化添加的组蛋白的蛋白激酶，其活性受到cAMP的刺激，而cAMP受体可能充当该激酶的调节亚基。膜蛋白也容易被内源性激酶磷酸化，表观分子量等于160×10 3 ，135×10 3 ，114×10 < sup> 3 ，并以58×10 3 为主要目标。其中114,000分子量的多肽可能与膜的质子转运ATPase相同。但是，cAMP依赖性蛋白激酶似乎不参与这些反应。完整的（ rho + 或 rho 0 ）细胞对质子电化学梯度在质膜上的消散作出反应如前所述（JM Trevillyan和ML Pall，J. Bacteriol。，> 138 ：397-403，1979）。因此，尽管酵母质膜包含刺激应答性腺苷酸环化酶系统的所有基本成分，但是偶联装置和涉及的靶标的精确性质仍有待确定。

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