University of Nottingham, School of Biology, University Park, Nottingham, UK.
FEBS Lett. 2011 Apr 6;585(7):1037-41. doi: 10.1016/j.febslet.2011.02.036. Epub 2011 Mar 3.
We have shown that the unfolded protein response (UPR) in Pichia pastoris requires splicing of a non-conventional intron in the HAC1(u) mRNA 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.
我们已经表明，毕赤酵母中的未折叠蛋白反应（UPR）需要在 HAC1(u)mRNA 中剪接一个非常规内含子，这与其他真核生物相同。毕赤酵母是一种受欢迎的酵母表达宿主，用于分泌生产异源蛋白，而毕赤酵母中 UPR 的调节可能是其有效折叠和分泌蛋白的关键。我们还表明，毕赤酵母的 Hac1p 的 C 末端区域是其功能所必需的。尽管来自酿酒酵母和毕赤酵母的 Hac1p 的 C 末端区域富含苯丙氨酸残基，但毕赤酵母的 Hac1p 缺乏一个 C 末端丝氨酸，已知该丝氨酸对酿酒酵母 Hac1p 的高效功能很重要。
