Walters Robert W, Parker Roy
Department of Chemistry and Biochemistry, University of Colorado at Boulder, Boulder, CO, USA.
Department of Chemistry and Biochemistry, University of Colorado at Boulder, Boulder, CO, USA; Howard Hughes Medical Institute, University of Colorado at Boulder, Boulder, CO, USA.
Trends Biochem Sci. 2015 Oct;40(10):552-559. doi: 10.1016/j.tibs.2015.08.004.
A key aspect of the control of gene expression is the differential rates of mRNA translation and degradation, including alterations due to extracellular inputs. Surprisingly, multiple examples now argue that Hsp70 protein chaperones and their associated Hsp40 partners modulate both mRNA degradation and translation. Hsp70 proteins affect mRNA metabolism by various mechanisms including regulating nascent polypeptide chain folding, activating signal transduction pathways, promoting clearance of stress granules, and controlling mRNA degradation in an mRNA-specific manner. Taken together, these observations highlight the general principle that mRNA metabolism is coupled to the proteostatic state of the cell, often as assessed by the presence of unfolded or misfolded proteins.
基因表达调控的一个关键方面是mRNA翻译和降解的差异速率，包括由于细胞外输入导致的改变。令人惊讶的是，现在有多个例子表明，热休克蛋白70（Hsp70）家族的蛋白质伴侣及其相关的Hsp40伴侣可调节mRNA的降解和翻译。Hsp70蛋白通过多种机制影响mRNA代谢，包括调节新生多肽链折叠、激活信号转导通路、促进应激颗粒的清除以及以mRNA特异性方式控制mRNA降解。综上所述，这些观察结果突出了一个普遍原则，即mRNA代谢与细胞的蛋白质稳态状态相关联，这通常通过未折叠或错误折叠蛋白质的存在来评估。
