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通过分子利用实现激素受体复杂性的进化。

Evolution of hormone-receptor complexity by molecular exploitation.

作者信息

Bridgham Jamie T, Carroll Sean M, Thornton Joseph W

机构信息

Center for Ecology and Evolutionary Biology, University of Oregon, Eugene, OR 97403, USA.

出版信息

Science. 2006 Apr 7;312(5770):97-101. doi: 10.1126/science.1123348.

DOI:10.1126/science.1123348
PMID:16601189
Abstract

According to Darwinian theory, complexity evolves by a stepwise process of elaboration and optimization under natural selection. Biological systems composed of tightly integrated parts seem to challenge this view, because it is not obvious how any element's function can be selected for unless the partners with which it interacts are already present. Here we demonstrate how an integrated molecular system-the specific functional interaction between the steroid hormone aldosterone and its partner the mineralocorticoid receptor-evolved by a stepwise Darwinian process. Using ancestral gene resurrection, we show that, long before the hormone evolved, the receptor's affinity for aldosterone was present as a structural by-product of its partnership with chemically similar, more ancient ligands. Introducing two amino acid changes into the ancestral sequence recapitulates the evolution of present-day receptor specificity. Our results indicate that tight interactions can evolve by molecular exploitation-recruitment of an older molecule, previously constrained for a different role, into a new functional complex.

摘要

根据达尔文理论,复杂性是在自然选择下通过逐步的细化和优化过程演化而来的。由紧密整合的部分组成的生物系统似乎对这一观点提出了挑战,因为除非与之相互作用的伙伴已经存在,否则不清楚任何元素的功能如何能够被选择。在这里,我们展示了一个整合的分子系统——类固醇激素醛固酮与其伙伴盐皮质激素受体之间的特定功能相互作用——是如何通过逐步的达尔文过程演化而来的。通过祖先基因复活,我们表明,早在激素演化之前,受体对醛固酮的亲和力就作为其与化学性质相似、更古老的配体相互作用的结构副产物而存在。在祖先序列中引入两个氨基酸变化概括了当今受体特异性的演化。我们的结果表明,紧密的相互作用可以通过分子利用——将一个以前因不同作用而受到限制的较老分子招募到一个新的功能复合体中——而演化。

相似文献

1
Evolution of hormone-receptor complexity by molecular exploitation.通过分子利用实现激素受体复杂性的进化。
Science. 2006 Apr 7;312(5770):97-101. doi: 10.1126/science.1123348.
2
Evolution. Reducible complexity.进化。可简化的复杂性。
Science. 2006 Apr 7;312(5770):61-3. doi: 10.1126/science.1126559.
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Molecular evolution. Resurrected proteins reveal their surprising history.分子进化。复活的蛋白质揭示了它们惊人的历史。
Science. 2007 Aug 17;317(5840):884-5. doi: 10.1126/science.317.5840.884b.
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Evolution of hormone selectivity in glucocorticoid and mineralocorticoid receptors.糖皮质激素和盐皮质激素受体中激素选择性的演变。
J Steroid Biochem Mol Biol. 2013 Sep;137:57-70. doi: 10.1016/j.jsbmb.2013.07.009. Epub 2013 Jul 29.
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Crystal structure of an ancient protein: evolution by conformational epistasis.一种古老蛋白质的晶体结构:通过构象上位性进行的进化
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Evolution of hormone signaling in elasmobranchs by exploitation of promiscuous receptors.通过利用混杂受体实现的板鳃亚纲动物激素信号的进化。
Mol Biol Evol. 2008 Dec;25(12):2643-52. doi: 10.1093/molbev/msn204. Epub 2008 Sep 17.
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A critical region in the mineralocorticoid receptor for aldosterone binding and activation by cortisol: evidence for a common mechanism governing ligand binding specificity in steroid hormone receptors.盐皮质激素受体中醛固酮结合及被皮质醇激活的关键区域:类固醇激素受体中调控配体结合特异性的共同机制的证据。
Mol Endocrinol. 2007 Apr;21(4):817-28. doi: 10.1210/me.2006-0246. Epub 2007 Feb 6.
8
Evolution of vertebrate steroid receptors from an ancestral estrogen receptor by ligand exploitation and serial genome expansions.脊椎动物类固醇受体通过配体利用和连续基因组扩张从祖先雌激素受体进化而来。
Proc Natl Acad Sci U S A. 2001 May 8;98(10):5671-6. doi: 10.1073/pnas.091553298. Epub 2001 May 1.
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Role of Pro-637 and Gln-642 in human glucocorticoid receptors and Ser-843 and Leu-848 in mineralocorticoid receptors in their differential responses to cortisol and aldosterone.Pro-637和Gln-642在人糖皮质激素受体中的作用以及Ser-843和Leu-848在盐皮质激素受体中对皮质醇和醛固酮的差异反应中的作用。
J Steroid Biochem Mol Biol. 2016 May;159:31-40. doi: 10.1016/j.jsbmb.2016.02.017. Epub 2016 Feb 22.
10
[Corticosteroid hormones: mechanisms involved in the recognition of aldosterone by mineralocorticoid receptors].[皮质类固醇激素:盐皮质激素受体识别醛固酮所涉及的机制]
J Soc Biol. 1999;193(4-5):355-60.

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