Su Ting-Yi, Harrison Paul M
Department of Biology, McGill University, Montreal, QC, Canada.
Front Mol Biosci. 2019 Jul 11;6:54. doi: 10.3389/fmolb.2019.00054. eCollection 2019.
Prions in eukaryotes have been linked to diseases, evolutionary capacitance, large-scale genetic control, and long-term memory formation. Prion formation and propagation have been studied extensively in the budding yeast . Here, we have analysed the conservation of sequence and of prion-like composition for prion-forming proteins and for other prion-like proteins from , across three evolutionary levels. We discover that prion-like status is well-conserved for about half the set of prion-formers at the level, and that prion-forming domains evolve more quickly as sequences than other prion-like domains do. Such increased mutation rates may be linked to the acquisition of functional roles for prion-forming domains during the evolutionary epoch of . Domain scores for prion-like composition in are strongly correlated with scores for such composition weighted evolutionarily over the dozens of fungal species examined, indicating conservation of such prion-like status. Examples of notable prion-like proteins that are highly conserved both in sequence and prion-like composition are discussed.
真核生物中的朊病毒与疾病、进化容量、大规模基因控制和长期记忆形成有关。朊病毒的形成和传播已在芽殖酵母中得到广泛研究。在这里，我们分析了三个进化水平上形成朊病毒的蛋白质以及其他朊病毒样蛋白质的序列保守性和朊病毒样组成。我们发现，在 水平上，约一半的朊病毒形成蛋白的朊病毒样状态保守性良好，并且与其他朊病毒样结构域相比，朊病毒形成结构域的序列进化更快。这种增加的突变率可能与 在进化时期朊病毒形成结构域功能作用的获得有关。 中朊病毒样组成的结构域得分与在所研究的数十种真菌物种中经进化加权的此类组成得分高度相关，表明这种朊病毒样状态的保守性。文中讨论了在序列和朊病毒样组成上都高度保守的显著朊病毒样蛋白质的例子。
