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果蝇热休克蛋白70(hsp70)基因3'端的缺失增加了热休克恢复过程中突变mRNA的稳定性。

A deletion of the 3' end of the Drosophila melanogaster hsp70 gene increases stability of mutant mRNA during recovery from heat shock.

作者信息

Simcox A A, Cheney C M, Hoffman E P, Shearn A

出版信息

Mol Cell Biol. 1985 Dec;5(12):3397-402. doi: 10.1128/mcb.5.12.3397-3402.1985.

Abstract

hsp40, an X-ray-induced deletion mutant of the major Drosophila melanogaster heat shock protein gene hsp70, was shown to be incorrectly regulated at the translational level. hsp40 protein synthesis persisted at a high level after the release from heat shock, whereas hsp70 protein production was rapidly repressed. This result was observed both in flies heterozygous for the hsp40 gene and in tissue culture cells transfected with the truncated gene. Analysis of the transcription of the hsp40 gene indicated that its mRNA, unlike hsp70 mRNA, was not actively destabilized after a return to control temperatures, permitting prolonged production of the mutant protein.

摘要

热休克蛋白40(hsp40)是黑腹果蝇主要热休克蛋白基因hsp70的一个X射线诱导缺失突变体,已证明其在翻译水平上调控异常。从热休克状态恢复后,hsp40蛋白质合成仍维持在高水平,而hsp70蛋白质的产生则迅速受到抑制。在hsp40基因杂合的果蝇以及转染了截短基因的组织培养细胞中均观察到了这一结果。对hsp40基因转录的分析表明,与hsp70 mRNA不同,其mRNA在恢复到对照温度后并未被积极地降解,从而使得突变蛋白得以长时间产生。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7db2/369168/ceca1d1736dc/molcellb00142-0076-a.jpg

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