大麦光系统II中醌和叶绿素a结合蛋白编码基因的一级结构。

E M Neumann
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引用次数: 11

摘要

在大麦叶绿体基因组中发现了编码醌结合D-1和D-2载脂蛋白和44 kD叶绿素a载脂蛋白3的psbA、psbD和psbC基因。它们被发现在叶绿体DNA的大单拷贝区域的23kbp的SalI限制性内切酶片段上,邻近反向重复。与其他物种一样,psbD和psbC基因的阅读框重叠了53 bp。它们在相同的方向上转录,但翻译时带有一个核苷酸的移码。将大麦、菠菜、烟草、豌豆和地菜进行比较,发现D-2多肽的18个n端残基中有10个氨基酸取代。D-2多肽的335个残基中只有8个取代。与紫色细菌和其他高等植物相比,大麦D-1和D-2蛋白中位于特殊对反应中心叶绿素推定结合位点的氨基酸残基和可能作为非血红素铁配体的氨基酸残基是严格保守的。在醌的结合中也观察到重要的残基的同一性。
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Primary structure of barley genes encoding quinone and chlorophyll a binding proteins of photosystem II.

The psbA, psbD and psbC genes encoding the quinone binding D-1 and D-2 apoproteins and the 44 kD chlorophyll a-apoprotein 3 have been located in the chloroplast genome of barley. They are found on a 23 kbp SalI restriction endonuclease fragment in the large single copy region of the chloroplast DNA adjacent to the inverted repeat. As in other species the psbD and psbC genes have reading frames which overlap by 53 bp. They are transcribed in the same direction but translated with a frameshift of one nucleotide. Ten amino acid substitutions are found among the 18 N-terminal residues of the D-2 polypeptide if barley, spinach, tobacco, pea and the liverwort Marchantia are compared. Only 8 substitutions are present among the 335 other residues of the D-2 polypeptide. The amino acid residues located in the putative binding site for the special pair reaction center chlorophyll and the residues probably serving as ligands to non-heme iron in the D-1 and D-2 proteins of barley are strictly conserved when compared to those of purple bacteria and of other higher plants. Identity is also observed for the residues of importance in the binding of quinones.

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