Alterations in the nuclear matrix protein mass correlate with heat-induced inhibition of DNA single-strand-break repair.

Alterations in the nuclear matrix protein mass correlate with heat-induced inhibition of DNA single-strand-break repair.
复制标题

核基质蛋白质量的变化与热诱导的 DNA 单链断裂修复抑制相关。

DOI:
10.1080/09553008714551761
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发表时间:
1987
期刊:
International journal of radiation biology and related studies in physics, chemistry, and medicine
影响因子:
--
通讯作者:
Lyons,BW
Lyons,BW
中科院分区:
--
文献类型:
--
作者:
Warters,RL;Brizgys,LM;Lyons,BW

文献摘要

被引文献

相似文献

观察到与来自中国仓鼠卵巢(CHO)细胞的核基质或类核共分离的总蛋白质质量在加热的细胞中随着在43°C和45°C之间增加暴露温度或在任何温度下暴露时间的增加而增加。CHO细胞类核在蔗糖梯度中的沉降距离随着45°C下暴露时间的增加而增加。这两个核的变化与热诱导的抑制DNA链断裂修复的对数线性方式相关。核基质蛋白质质量的两倍阈值增加先于DNA单链断裂修复的任何实质性抑制。当预热细胞(45°C,15分钟)在37°C下孵育时,核基质蛋白质质量和类核沉降以约5小时的半衰期恢复,而DNA单链断裂修复以约2小时的半衰期恢复。当将预热的细胞置于41°C(降压加热; SDH)时,观察到核基质蛋白质质量和DNA链断裂修复的半衰期进一步增加,而类核沉降恢复到对照值。这些结果表明,在热诱导的抑制DNA单链断裂修复的核基质的蛋白质质量的变化。
The total protein mass co-isolating with the nuclear matrix or nucleoid from Chinese hamster ovary (CHO) cells was observed to increase in heated cells as a function of increasing exposure temperature between 43°C and 45°C or of exposure time at any temperature. The sedimentation distance of the CHO cell nucleoid in sucrose gradients increased with increasing exposure time at 45°C. Both these nuclear alterations correlated in a log-linear manner with heat-induced inhibition of DNA strand break repair. A two-fold threshold increase in nuclear matrix protein mass preceded any substantial inhibition of repair of DNA single-strand breaks. When preheated cells (45°C for 15 min) were incubated at 37°C the nuclear matrix protein mass and nucleoid sedimentation recovered with a half-time of about 5 h, while DNA single-strand-break repair recovered with a half-time of about 2 h. When preheated cells were placed at 41°C (step-down heating; SDH) a further increase was observed in the nuclear matrix protein mass and the half-time of DNA strand break repair, while nucleoid sedimentation recovered toward control values. These results implicate alterations in the protein mass of the nuclear matrix in heat-induced inhibition of repair of DNA single-strand breaks.