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构巢曲霉的蛋白激酶C(PkcA)参与青霉素的产生。

Protein kinase C (PkcA) of Aspergillus nidulans is involved in penicillin production.

作者信息

Herrmann Martina, Spröte Petra, Brakhage Axel A

机构信息

Department of Molecular and Applied Microbiology, Leibniz Institute for Natural Product Research and Infection Biology (HKI), Beutenbergstrasse 11a, D-07745 Jena, Germany.

出版信息

Appl Environ Microbiol. 2006 Apr;72(4):2957-70. doi: 10.1128/AEM.72.4.2957-2970.2006.

Abstract

The biosynthesis of the beta-lactam antibiotic penicillin in the filamentous fungus Aspergillus nidulans is catalyzed by three enzymes that are encoded by the acvA, ipnA, and aatA genes. A variety of cis-acting DNA elements and regulatory factors form a complex regulatory network controlling these beta-lactam biosynthesis genes. Regulators involved include the CCAAT-binding complex AnCF and AnBH1. AnBH1 acts as a repressor of the penicillin biosynthesis gene aatA. Until now, however, little information has been available on the signal transduction cascades leading to the transcription factors. Here we show that inhibition of protein kinase C (Pkc) activity in A. nidulans led to cytoplasmic localization of an AnBH1-enhanced green fluorescent protein (EGFP) fusion protein. Computer analysis of the genome and screening of an A. nidulans gene library revealed that the fungus possesses two putative Pkc-encoding genes, which we designated pkcA and pkcB. Only PkcA showed all the characteristic features of fungal Pkc's. Production of pkcA antisense RNA in A. nidulans led to reduced growth and conidiation in Aspergillus minimal medium, while in fermentation medium it led to enhanced expression of an aatAp-lacZ gene fusion, reduced pencillin production, and predominantly cytoplasmic localization of AnBH1. These data agree with the finding that inhibition of Pkc activity prevented nuclear localization of AnBH1-EGFP. As a result, repression of aatA expression was relieved. The involvement of Pkc in penicillin biosynthesis is also interesting in light of the fact that in the yeast Saccharomyces cerevisiae, Pkc plays a major role in maintaining cell integrity.

摘要

丝状真菌构巢曲霉中β-内酰胺抗生素青霉素的生物合成由acvA、ipnA和aatA基因编码的三种酶催化。多种顺式作用DNA元件和调控因子形成一个复杂的调控网络,控制这些β-内酰胺生物合成基因。涉及的调控因子包括CCAAT结合复合物AnCF和AnBH1。AnBH1作为青霉素生物合成基因aatA的阻遏物。然而,到目前为止,关于导致转录因子的信号转导级联的信息还很少。在这里我们表明,抑制构巢曲霉中的蛋白激酶C(Pkc)活性导致AnBH1增强绿色荧光蛋白(EGFP)融合蛋白定位于细胞质。对基因组的计算机分析和构巢曲霉基因文库的筛选表明,该真菌拥有两个假定的编码Pkc的基因,我们将其命名为pkcA和pkcB。只有PkcA表现出真菌Pkc的所有特征。在构巢曲霉中产生pkcA反义RNA导致在曲霉基本培养基中生长和产孢减少,而在发酵培养基中则导致aatAp-lacZ基因融合体的表达增强、青霉素产量降低以及AnBH1主要定位于细胞质。这些数据与抑制Pkc活性阻止AnBH1-EGFP核定位的发现一致。结果,aatA表达的抑制被解除。鉴于在酿酒酵母中Pkc在维持细胞完整性中起主要作用,Pkc参与青霉素生物合成也很有趣。

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