KARYOPHILIC PROTEINS - POLYPEPTIDES SYNTHESIZED INVITRO ACCUMULATE IN THE NUCLEUS ON MICRO-INJECTION INTO THE CYTOPLASM OF AMPHIBIAN OOCYTES

KARYOPHILIC PROTEINS - POLYPEPTIDES SYNTHESIZED INVITRO ACCUMULATE IN THE NUCLEUS ON MICRO-INJECTION INTO THE CYTOPLASM OF AMPHIBIAN OOCYTES
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DOI:
10.1073/pnas.79.17.5302
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发表时间:
1982-01-01
期刊:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES
影响因子:
--
通讯作者:
FRANKE, WW
FRANKE, WW
中科院分区:
其他
文献类型:
--
作者:
DABAUVALLE, MC;FRANKE, WW

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研究了不同两栖动物[非洲爪蟾(Xenopus laevis)、临时蛙(Rana temporaria)、美洲蛙(Rana esculenta)和华氏侧耳(Pleurodeles waltlii)]卵母细胞中一些主要可溶性酸性核蛋白的特异性核细胞质区隔化。利用青蛙X. laevis卵巢mRNA体外翻译合成并放射性标记的蛋白质,注射到非洲爪蟾(Xenopus)或华氏蝾螈(salamander P. waltlii)活卵母细胞的细胞质中。注射后不同时间手工分离细胞核和细胞质,用二维凝胶电泳分析内源蛋白和注射蛋白。几种主要的大小和电荷不同的核特异性蛋白质,包括非常酸性的蛋白质N1和N2 (MW, 110,000和100,000)和N4 (MW, 34,000),在这两种形式中都是相同的。在体外作为翻译产物和存在于核质中。这些核蛋白的细胞质前体形式不存在显著差异。翻译产物包含指示这些蛋白质在细胞核内特异性隔离的信号;这些蛋白质在核质中积累不需要翻译后加工;这些信号和机制并不是物种特有的。
The specific nucleocytoplasmic compartmentalization of proteins was examined for some major soluble acidic nuclear proteins in oocytes of different amphibia [Xenopus laevis, Rana temporaria, Rana esculenta and Pleurodeles waltlii]. Proteins synthesized and radioactively labeled by translation in vitro, by using mRNA from ovaries of the frog X. laevis, were injected into the cytoplasm of living oocytes of Xenopus or of the salamander P. waltlii. At various times after injection, nucleus and cytoplasm were manually separated and endogenous and injected proteins were analyzed by 2-dimensional gel electrophoresis. Several major nucleus-specific proteins of different sizes and electrical charges, including the very acidic proteins N1 and N2 (MW, 110,000 and 100,000) and N4 (MW 34,000), are identical in both forms.sbd.i.e., as translation products in vitro and as present in the nucleoplasm. Significantly different cytoplasmic precursor forms to these nuclear proteins do not exist. The translation products contain the signal(s) directing the specific sequestration of these proteins within the nucleus; post-translational processing is not required for the accumulation of these proteins in the nucleoplasm; and the signals and the mechanisms involved are not species specific.