一个对称蛋白质的De Novo进化出现是由折叠约束所塑造的
Robert G Smock1, Itamar Yadid2, Orly Dym1
1Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
Cell
|January 26, 2016
概括
像β螺旋一样, 新的蛋白质折叠从复制和演变的小图案中出现. 提高折叠效率推动了这一功能性的出现,克服了最初的组装挑战.
科学领域:
- 分子生物学
- 进化生物学
- 结构生物学
背景情况:
- 结构上不同的蛋白质折叠的新出现仍然不太清楚.
- 分子进化研究主要关注功能差异,而不是新型蛋白质结构的起源.
研究的目的:
- 调查贝塔螺旋蛋白出现的进化轨迹和选择压力.
- 了解小,重复的图案如何组装和演变为复杂的功能性蛋白质结构.
主要方法:
- 在基因组数据中识别短的螺旋形图案.
- 祖先蛋白质图案的遗传重建
- 在折叠过程中对进化力量和折叠约束的分析.
主要成果:
- 发现短基因 (<50个氨基酸) 通过串联重复扩展以形成现有的β螺旋.
- 重建了47个遗留的原始图案,显示它们被组装成五叶甲状螺旋.
- 一个功能性轨迹证明了导致单体单体的双重复制,而可折叠性是改善功能的关键驱动因素.
结论:
- 在贝塔螺旋的进化过程中,可折叠性是增强蛋白质功能的主要因素.
- 早期的进化阶段受到单体折叠和小分子组合之间的冲突的限制.
- 后来的阶段,即双重复制后,涉及单体稳定性和可折叠性之间的权衡.
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