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与光合系统 II 光合放氧相关的多肽的细胞内编码位点。

Intracellular coding sites of polypeptides associated with photosynthetic oxygen evolution of photosystem II.

机构信息

Botanisches Institut der Universität, Universitätsstraße 1, 4 Düsseldorf 1, FRG.

出版信息

Plant Mol Biol. 1985 Mar;4(2-3):137-46. doi: 10.1007/BF02418761.

Abstract

Three hydrophilic polypeptides of approximately 34, 23, and 16 kd located on the inner thylakoid surface are associated with the water-splitting activity of photosystem II. Stable transcripts for the three proteins were found only in cytosolic (polyadenylated) RNA, suggesting that they are encoded in nuclear genes. The immunologically reacting products synthesized in a rabbit reticulocyte cell-free translation system are larger in size than the authentic mature proteins by about 6-10 kd. These larger precursors are imported post-translationally into isolated, intact chloroplasts, and are processed to their mature forms during or after translocation. The imported proteins can be extracted from thylakoids by procedures used to isolate the three native proteins of the water-splitting complex, suggesting that they have assembled properly into their final destination, the inner thylakoid surface.

摘要

三个亲水性多肽,分子量约为 34、23 和 16kDa,位于类囊体的内表面,与光系统 II 的水分解活性有关。只有在细胞质(多聚腺苷酸化)RNA 中发现这三种蛋白质的稳定转录本,表明它们是由核基因编码的。在兔网织红细胞无细胞翻译系统中合成的免疫反应产物比真实成熟蛋白大约大 6-10kDa。这些较大的前体在后翻译过程中被导入到分离的完整叶绿体中,并在转运过程中或之后被加工成成熟形式。从类囊体中提取的蛋白质可以通过用于分离水分解复合物的三种天然蛋白质的程序来提取,这表明它们已经正确地组装到最终目的地,即类囊体的内表面。

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