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热休克诱导果蝇核糖体蛋白的快速去磷酸化。

Heat shock induces rapid dephosphorylation of a ribosomal protein in Drosophila.

作者信息

Glover C V

出版信息

Proc Natl Acad Sci U S A. 1982 Mar;79(6):1781-5. doi: 10.1073/pnas.79.6.1781.

Abstract

Ribosomes isolated from Drosophila melanogaster tissue culture cells labeled in vivo with 32Pi contain a single, heavily phosphorylated, ribosomal protein. As much as 40% of this protein is phosphorylated in cells cultured at 25 degrees C. The molecular weight and other characteristics of this protein suggest possible homology with ribosomal protein S6. Following a shift-up to 37 degrees C, the protein is specifically and quantitatively dephosphorylated. The kinetics of this dephosphorylation are rapid with a half-time on the order of a few minutes. These kinetics closely parallel the heat shock-induced breakdown of the preexisting polysome population.

摘要

从用³²Pᵢ在体内标记的黑腹果蝇组织培养细胞中分离出的核糖体含有一种单一的、高度磷酸化的核糖体蛋白。在25摄氏度培养的细胞中,多达40%的这种蛋白被磷酸化。这种蛋白的分子量和其他特性表明它可能与核糖体蛋白S6具有同源性。温度升至37摄氏度后,该蛋白会被特异性地定量去磷酸化。这种去磷酸化的动力学很快,半衰期约为几分钟。这些动力学与热休克诱导的现有多核糖体群体的分解密切平行。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2fee/346064/4997ac9beba9/pnas00445-0108-a.jpg

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