Interacting proteins on human spermatozoa: adaptive evolution of the binding of semenogelin I to EPPIN.
Interacting proteins on human spermatozoa: adaptive evolution of the binding of semenogelin I to EPPIN.
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DOI：
10.1371/journal.pone.0082014
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发表时间：
2013
期刊：
影响因子：
3.7
通讯作者：
O'Rand MG
中科院分区：
文献类型：
--
作者：
Silva EJ;Hamil KG;O'Rand MG
精液凝固蛋白I（SEMG 1）存在于人精液凝固物和与EPPIN结合的精子表面。精子表面SEMG 1/EPPIN相互作用的生理意义在于其调节精子前向运动的能力。本研究调查的假设，表面的SEMG 1和EPPIN共同进化的Hominoidea的时间尺度内，作为一个适应性的压力施加的作用，在精子保护和生殖健康。我们的研究结果表明，SEMG 1和EPPIN的一些氨基酸残基具有显着的缺乏变异之间的类人猿。我们观察到一个独特的残基变化，人类特有的EPPIN序列内含有表面肌电蛋白1相互作用的表面，即His 92。此外，正选择的贝叶斯经验贝叶斯分析表明，SEMG 1 Cys 239残基在人类中经历了正选择，可能是由于其在增加这些相互作用蛋白的结合亲和力中的作用。我们证实了Cys 239残基的SEMG 1结合EPPIN和精子活力的抑制的关键作用，通过显示重组SEMG 1突变体，其中Cys 239残基改变为甘氨酸，天冬氨酸，组氨酸，丝氨酸或精氨酸有能力降低相互作用的EPPIN和抑制人精子活力在体外。总之，我们的研究结果表明，EPPIN和SEMG 1在灵长类动物中迅速共同进化，因为它们在精液凝固物中调节精子运动力的关键作用，为精子表面相互作用蛋白的分子共同进化提供了独特的见解。
Semenogelin I (SEMG1) is found in human semen coagulum and on the surface of spermatozoa bound to EPPIN. The physiological significance of the SEMG1/EPPIN interaction on the surface of spermatozoa is its capacity to modulate sperm progressive motility. The present study investigates the hypothesis that the interacting surface of SEMG1 and EPPIN co-evolved within the Hominoidea time scale, as a result of adaptive pressures applied by their roles in sperm protection and reproductive fitness. Our results indicate that some amino acid residues of SEMG1 and EPPIN possess a remarkable deficiency of variation among hominoid primates. We observe a distinct residue change unique to humans within the EPPIN sequence containing a SEMG1 interacting surface, namely His92. In addition, Bayes Empirical Bayes analysis for positive selection indicates that the SEMG1 Cys239 residue underwent positive selection in humans, probably as a consequence of its role in increasing the binding affinity of these interacting proteins. We confirm the critical role of Cys239 residue for SEMG1 binding to EPPIN and inhibition of sperm motility by showing that recombinant SEMG1 mutants in which Cys239 residue was changed to glycine, aspartic acid, histidine, serine or arginine have reduced capacity to interact to EPPIN and to inhibit human sperm motility in vitro. In conclusion, our results indicate that EPPIN and SEMG1 rapidly co-evolved in primates due to their critical role in the modulation of sperm motility in the semen coagulum, providing unique insights into the molecular co-evolution of sperm surface interacting proteins.
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影响因子：
3.6
作者：
O'Rand, Michael G.;Widgren, Esther E.
通讯作者：
Widgren, Esther E.
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