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谷氨酸合酶在一种红藻中由质体编码:对谷氨酸合酶进化的启示。

Glutamate synthase is plastid-encoded in a red alga: implications for the evolution of glutamate synthases.

作者信息

Valentin K, Kostrzewa M, Zetsche K

机构信息

Institute for Plant Physiology, Giessen, Germany.

出版信息

Plant Mol Biol. 1993 Oct;23(1):77-85. doi: 10.1007/BF00021421.

Abstract

An actively transcribed gene (glsF) encoding for ferredoxin-dependent glutamate synthase (Fd-GOGAT) was found on the plastid genome of the multicellular red alga Antithamnion sp. Fd-GOGAT is not plastid-encoded in chlorophytic plants, demonstrating that red algal plastid genomes encode for additional functions when compared to those known from green chloroplasts. Moreover, our results suggest that the plant Fd-GOGAT has an endosymbiotic origin. The same may not be true for NADPH-dependent GOGAT. In Antithamnion glsF is flanked upstream by cpcBA and downstream by psaC and is transcribed monocistronically. Implications of these results for the evolution of GOGAT enzymes and the plastid genome are discussed.

摘要

在多细胞红藻Antithamnion sp.的质体基因组上发现了一个编码铁氧化还原蛋白依赖性谷氨酸合酶(Fd-GOGAT)的活跃转录基因(glsF)。在绿藻植物中,Fd-GOGAT不是由质体编码的,这表明与已知的绿色叶绿体相比,红藻质体基因组编码了更多功能。此外,我们的结果表明植物Fd-GOGAT具有内共生起源。对于NADPH依赖性GOGAT可能并非如此。在Antithamnion中,glsF的上游侧翼是cpcBA,下游侧翼是psaC,并且以单顺反子形式转录。讨论了这些结果对GOGAT酶进化和质体基因组的影响。

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