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植物生长调节蛋白相互作用特异性的进化。

Evolution of a plant growth-regulatory protein interaction specificity.

机构信息

Department of Biology, University of Oxford, Oxford, UK.

State Key Laboratory of Plant Cell and Chromosome Engineering, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, P. R. China.

出版信息

Nat Plants. 2023 Dec;9(12):2059-2070. doi: 10.1038/s41477-023-01556-0. Epub 2023 Oct 30.

DOI:10.1038/s41477-023-01556-0
PMID:37903985
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10724065/
Abstract

Specific protein-protein interactions (PPIs) enable biological regulation. However, the evolution of PPI specificity is little understood. Here we trace the evolution of the land-plant growth-regulatory DELLA-SLY1/GID2 PPI, revealing progressive increase in specificity of affinity of SLY1/GID2 for a particular DELLA form. While early-diverging SLY1s display relatively broad-range DELLA affinity, later-diverging SLY1s tend towards increasingly stringent affinity for a specific DELLA A' form generated by the growth-promoting phytohormone gibberellin (GA). Our novel mutational strategy reveals amino acid substitutions contributing to the evolution of Arabidopsis thaliana SLY1 A' specificity, also showing that routes permitting reversion to broader affinity became increasingly constrained over evolutionary time. We suggest that progressive affinity narrowing may be an important evolutionary driver of PPI specificity and that increase in SLY1/GID2-DELLA specificity enabled the enhanced flexibility of plant physiological environmental adaptation conferred by the GA-DELLA growth-regulatory mechanism.

摘要

特定的蛋白质-蛋白质相互作用（PPIs）使生物能够进行调控。然而，PPIs 特异性的进化仍知之甚少。在这里，我们追踪了陆地植物生长调节蛋白 DELLA-SLY1/GID2 PPI 的进化过程，揭示了 SLY1/GID2 与特定 DELLA 形式的亲和力特异性逐渐增加。虽然早期分化的 SLY1 显示出相对广泛的 DELLA 亲和力，但后来分化的 SLY1 则倾向于对由生长促进植物激素赤霉素（GA）产生的特定 DELLA A'形式表现出越来越严格的亲和力。我们的新突变策略揭示了导致拟南芥 SLY1 A'特异性进化的氨基酸取代，也表明允许回复到更广泛亲和力的途径在进化过程中受到越来越多的限制。我们认为，亲和力的逐渐变窄可能是 PPI 特异性进化的一个重要驱动因素，并且 SLY1/GID2-DELLA 特异性的增加使 GA-DELLA 生长调节机制赋予的植物生理环境适应的灵活性得到增强。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc62/10724065/b3d25985721a/41477_2023_1556_Fig13_ESM.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc62/10724065/16c375418d4a/41477_2023_1556_Fig7_ESM.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc62/10724065/11641e21c1a4/41477_2023_1556_Fig9_ESM.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc62/10724065/45883e401248/41477_2023_1556_Fig10_ESM.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc62/10724065/b3d25985721a/41477_2023_1556_Fig13_ESM.jpg

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AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models.AlphaFold 蛋白质结构数据库：用高精度模型极大地扩展蛋白质序列空间的结构覆盖范围。
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