Recombination of protein domains facilitated by co-translational folding in eukaryotes
Recombination of protein domains facilitated by co-translational folding in eukaryotes
复制标题
DOI：
10.1038/41024
复制
发表时间：
1997-07-24
期刊：
影响因子：
64.8
通讯作者：
Hartl, FU
中科院分区：
文献类型：
--
作者：
Netzer, WJ;Hartl, FU
复杂基因组的进化需要预先存在的蛋白质结构域的新组合成功地折叠成模块化多肽。在真核翻译模型中，双结构域多肽通过其结构域的顺序折叠和共翻译折叠而有效地折叠。相反，相同蛋白质在大肠杆菌中的折叠是翻译后的，并导致同时折叠结构域的分子内错误折叠。真核生物中的顺序结构域折叠可能在模块化多肽的进化中起到关键作用，因为它增加了随机基因融合事件导致可立即折叠的蛋白质结构的概率。
The evolution of complex genomes requires that new combinations of pre-existing protein domains successfully fold into modular polypeptides. During eukaryotic translation model two-domain polypeptides fold efficiently by sequential and co-translational folding of their domains. In contrast, folding of the same proteins in Escherichia coli is post-translational, and leads to intramolecular misfolding of concurrently folding domains. Sequential domain folding in eukaryotes may have been critical in the evolution of modular polypeptides, by increasing the probability that random gene-fusion events resulted in immediately foldable protein structures.