Adaptive and degenerative evolution of the S-Phase Kinase-Associated Protein 1-Like family in Arabidopsis thaliana
Adaptive and degenerative evolution of the S-Phase Kinase-Associated Protein 1-Like family in Arabidopsis thaliana
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DOI：
10.7717/peerj.6740
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发表时间：
2019-04-12
期刊：
影响因子：
2.7
通讯作者：
Gao, Zhenyu
中科院分区：
文献类型：
--
作者：
Hua, Zhihua;Gao, Zhenyu
基因组测序发现了物种内部和物种之间的巨大序列变异。在植物中，除了基因组大小的巨大变化之外，在几个大的多基因家族中也明显存在大量的序列多态性，包括参与泛素-26S蛋白酶体蛋白降解系统的那些。然而，这种序列变异的生物学功能尚不清楚。在这项工作中，我们明确证明了一个单一的起源逆转拟南芥Skp 1-Like（ASK）基因使用改进的系统发育分析。利用1，001基因组项目，我们在这里提供了几行多态性证据，显示了ASK基因的适应性和退行性进化过程。酵母双杂交定量相互作用分析进一步表明，最近中性的变化，在ASK 2编码序列削弱了它与一些F盒蛋白的相互作用。ASK 1上游高度多态性区域产生高水平表达的趋势暗示了ASK 1通过一种未知的转录抑制机制进行负表达调控，这可能有助于Skp 1-CUL 1-F-box复合物的多态性作用。总之，这项研究提供了新的进化证据，以指导未来的SCF介导的蛋白质泛素化的功能基因组学研究。
Genome sequencing has uncovered tremendous sequence variation within and between species. In plants, in addition to large variations in genome size, a great deal of sequence polymorphism is also evident in several large multi-gene families, including those involved in the ubiquitin-26S proteasome protein degradation system. However, the biological function of this sequence variation is yet not clear. In this work, we explicitly demonstrated a single origin of retroposed Arabidopsis Skp1-Like (ASK) genes using an improved phylogenetic analysis. Taking advantage of the 1,001 genomes project, we here provide several lines of polymorphism evidence showing both adaptive and degenerative evolutionary processes in ASK genes. Yeast two-hybrid quantitative interaction assays further suggested that recent neutral changes in the ASK2 coding sequence weakened its interactions with some F-box proteins. The trend that highly polymorphic upstream regions of ASK1 yield high levels of expression implied negative expression regulation of ASK1 by an as-yet-unknown transcriptional suppression mechanism, which may contribute to the polymorphic roles of Skp1 -CUL1-F-box complexes. Taken together, this study provides new evolutionary evidence to guide future functional genomic studies of SCF-mediated protein ubiquitylation.