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首页> 外文期刊>Biochemistry >Interactions of the Acyl Chain with the Saccharomyces cerevisiae Acyl Carrier Protein
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Interactions of the Acyl Chain with the Saccharomyces cerevisiae Acyl Carrier Protein

机译：酰基链与酿酒酵母酰基载体蛋白的相互作用

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摘要

Acyl carrier protein (ACP) domains are critical integral components 0 OH of multifunctional type I fatty acid synthases (FAS I) and polyketide synthases (PKSs), where they shuttle the growing adducts of the synthesis between the catalytic domains. In contrast to ACP of mammalian FAS I, PKSs, and the dissociated fatty acid synthase type II ystems (FAS II) of bacteria, fungal FAS I ACP consists of two subdomains, one comprising the canonical ACP fold observed in all FAS systems and the other representing an extra structural subdomain. While ACPs of dissociated FAS II are able to sequester the reaction intermediates during substrate shuttling, such a transport mechanism has not been observed in ACP domains of multifunctional FAS I and PKS systems. For a better understanding of the interaction between the canonical subdomain of fungal ACP with the growing acyl chain and the role of the structural sub domain, we determined the structure of the isolated SaccharomyceS cerevisiae acyl carrier protein (ScACP) domain by NMR spectroscopy and investigated the interactions between ScACP and covalently attached substrate acyl chains of varying length by monitoring chemical shift perturbations. The interactions were mapped to the hydrophobic core of the canonical subdomain, while no perturbations were detected in the structural subdomain. A population analysis revealed that only approximately 15% of covalently attached decanoyl chains ate sequestered by the ACP tore, comparable to the mammalian FAS I and multifunctional PKS systems, which do not sequester their substrates. Finally, denaturation experiments show that both ScACP subdomains unfold cooperatively and that the weak interaction of the acyl chain with the hydrophobic core does not significantly affect the ACP stability.
机译：酰基载体蛋白（ACP）域是多功能I型脂肪酸合酶（FAS I）和聚酮化合物合酶（PKS）的关键组成部分0 OH，它们在催化域之间穿梭合成中不断增长的加合物。与哺乳动物FAS I，PKSs的ACP和细菌的解离的II型脂肪酸合酶系统（FAS II）相比，真菌FAS I ACP由两个子域组成，一个包含在所有FAS系统中观察到的规范ACP折叠，另一个代表一个额外的结构子域。尽管解离的FAS II的ACP能够隔离底物穿梭过程中的反应中间体，但在多功能FAS I和PKS系统的ACP域中尚未观察到这种转运机制。为了更好地了解真菌ACP的规范子结构域与增长的酰基链之间的相互作用以及结构子结构域的作用，我们通过NMR光谱确定了分离的酿酒酵母酰基载体蛋白（ScACP）域的结构，并研究了通过监测化学位移扰动，使ScACP与不同长度的共价连接的底物酰基链之间发生相互作用。相互作用被映射到规范子域的疏水核心，而在结构子域中未检测到扰动。人口分析显示，与不将其底物螯合的哺乳动物FAS I和多功能PKS系统相比，ACP只能隔离约15％的共价连接的癸酰基链。最后，变性实验表明两个ScACP子域协同展开，并且酰基链与疏水核的弱相互作用不会显着影响ACP的稳定性。

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