Activation of the unfolded protein response in Pichia pastoris requires splicing of a HAC1 mRNA intron and retention of the C-terminal tail of Hac1p.
Activation of the unfolded protein response in Pichia pastoris requires splicing of a HAC1 mRNA intron and retention of the C-terminal tail of Hac1p.
复制标题
毕赤酵母中未折叠蛋白反应的激活需要 HAC1 mRNA 内含子的剪接和 Hac1p C 末端尾部的保留。
DOI：
10.1016/j.febslet.2011.02.036
复制
发表时间：
2011
期刊：
影响因子：
3.5
通讯作者：
Whyteside G
中科院分区：
文献类型：
--
作者：
Whyteside G
我们已经表明，在巴斯德毕赤酵母中的未折叠蛋白质反应（UPR）需要与其他真核生物一样，在HAC 1umRNA中剪接一个非常规内含子。巴斯德毕赤酵母是分泌生产异源蛋白的理想酵母表达宿主，其UPR的调控可能是其有效折叠和分泌蛋白的关键。我们还表明，来自巴斯德毕赤酵母的Hac 1 p的C-末端区域是功能所必需的。虽然两种S.酿酒酵母和巴斯德毕赤酵母富含苯丙氨酸残基，巴斯德毕赤酵母Hac 1 p缺乏C-末端丝氨酸，已知该丝氨酸在来自酿酒酵母的Hac 1 p的有效功能中是重要的。啤酒。
We have shown that the unfolded protein response (UPR) in Pichia pastoris requires splicing of a non-conventional intron in the HAC1umRNA in common with other eukaryotes. P. pastoris is a favoured yeast expression host for secreted production of heterologous proteins and the regulation of the UPR in P. pastoris may hold the key to its effective folding and secretion of proteins. We have also shown that the C-terminal region of the Hac1p from P. pastoris is required for functionality. Although the C-terminal regions of Hac1p from both S. cerevisiae and P. pastoris are rich in phenylalanine residues, the P. pastoris Hac1p lacks a C-terminal serine that is known to be important in the efficient functionality of Hac1p from S. cerevisiae.