Hauburger Anja, Kliemannel Marco, Madsen Peder, Rudolph Rainer, Schwarz Elisabeth
Institut für Biotechnologie der Martin-Luther-Universität Halle-Wittenberg, Kurt-Mothes-Strasse 3, 06120 Halle, Germany.
FEBS Lett. 2007 Sep 4;581(22):4159-64. doi: 10.1016/j.febslet.2007.07.063. Epub 2007 Aug 6.
We have previously shown that the pro-peptide of human nerve growth factor (NGF) facilitates oxidative folding of the mature part. For the analysis of functional specificities of the pro-peptides of NGF and the related neurotrophin-3 (NT-3) with respect to structure formation, chimeric proteins with swapped pro-peptides were generated. Neither the structure nor the stability of the mature domains was influenced by the heterologous pro-peptides. For the pro-peptide of NT-3 fused to the mature part of NGF, stabilization of the pro-peptide moiety by the NGF part was observed. Folding kinetics and renaturation yields of this chimeric protein were comparable to those of proNGF. Our results demonstrate functional interchangeability between the pro-peptides of NGF and NT-3 with respect to their role in assisting oxidative folding of the mature part.
我们之前已经表明，人类神经生长因子（NGF）的前肽促进成熟部分的氧化折叠。为了分析NGF和相关神经营养因子-3（NT-3）的前肽在结构形成方面的功能特异性，构建了前肽互换的嵌合蛋白。异源前肽既不影响成熟结构域的结构，也不影响其稳定性。对于与NGF成熟部分融合的NT-3前肽，观察到NGF部分对前肽部分有稳定作用。这种嵌合蛋白的折叠动力学和复性产率与前NGF相当。我们的结果表明，NGF和NT-3的前肽在协助成熟部分氧化折叠的作用方面具有功能互换性。
