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双链DNA可诱导动物细胞提取物中包括90000分子量热休克蛋白在内的几种蛋白质发生磷酸化。

Double-stranded DNA induces the phosphorylation of several proteins including the 90 000 mol. wt. heat-shock protein in animal cell extracts.

作者信息

Walker A I, Hunt T, Jackson R J, Anderson C W

出版信息

EMBO J. 1985 Jan;4(1):139-45. doi: 10.1002/j.1460-2075.1985.tb02328.x.

DOI:10.1002/j.1460-2075.1985.tb02328.x
PMID:4018025
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC554162/
Abstract

Double-stranded DNA (dsDNA) induces the transfer of phosphate from ATP to several proteins in extracts of widely divergent eukaryotic cells. Extracts of HeLa cells, rabbit reticulocytes, Xenopus eggs and Arbacia eggs all show dsDNA-dependent protein phosphorylation. The mechanism is specific for dsDNA and will not respond to either RNA or single-stranded DNA. One of the proteins which is phosphorylated in response to dsDNA has a subunit mol. wt. of 90 000 and has been identified as a heat-shock protein (hsp90). Although mouse cell extracts were shown to contain hsp90, they failed to show a dsDNA-dependent protein phosphorylation. The observation that dsDNA can modulate the phosphorylation of a set of proteins raises the possibility that dsDNA may play a role as a cellular regulatory signal.

摘要

双链DNA（dsDNA）可诱导从ATP转移磷酸基团至多种差异极大的真核细胞提取物中的蛋白质。人宫颈癌细胞（HeLa细胞）、兔网织红细胞、非洲爪蟾卵和海胆卵的提取物均显示出dsDNA依赖性蛋白磷酸化。该机制对dsDNA具有特异性，对RNA或单链DNA均无反应。响应dsDNA而被磷酸化的一种蛋白质的亚基分子量为90000，已被鉴定为热休克蛋白（hsp90）。尽管已证明小鼠细胞提取物含有hsp90，但未显示出dsDNA依赖性蛋白磷酸化。dsDNA可调节一组蛋白质磷酸化这一观察结果增加了dsDNA可能作为细胞调节信号发挥作用的可能性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a532/554162/e3976ab88d22/emboj00266-0144-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a532/554162/fa4a8087eb13/emboj00266-0141-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a532/554162/a0aed553f884/emboj00266-0141-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a532/554162/702a8a08eda2/emboj00266-0142-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a532/554162/82db87f68d05/emboj00266-0143-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a532/554162/e3976ab88d22/emboj00266-0144-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a532/554162/fa4a8087eb13/emboj00266-0141-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a532/554162/a0aed553f884/emboj00266-0141-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a532/554162/702a8a08eda2/emboj00266-0142-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a532/554162/82db87f68d05/emboj00266-0143-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a532/554162/e3976ab88d22/emboj00266-0144-a.jpg

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Kinase Activity of PAR1b, Which Mediates Nuclear Translocation of the BRCA1 Tumor Suppressor, Is Potentiated by Nucleic Acid-Mediated PAR1b Multimerization.PAR1b 激酶活性可介导 BRCA1 肿瘤抑制因子的核易位，该活性可通过核酸介导的 PAR1b 多聚化增强。
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