Nan Fangru, Han Yuxin, Liu Xudong, Feng Jia, Lv Junping, Liu Qi, Xie Shulian
{"title":"红藻属rbcL基因的适应进化与协同进化分析。","authors":"Nan Fangru, Han Yuxin, Liu Xudong, Feng Jia, Lv Junping, Liu Qi, Xie Shulian","doi":"10.1177/1176934320977862","DOIUrl":null,"url":null,"abstract":"<p><p>The adaptive evolution and coevolution of the ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit (<i>rbc</i>L) gene in the genus <i>Hildenbrandia</i> were studied based on phylogenetic tree construction and the physicochemical properties and the secondary structures of protein encoded by <i>rbc</i>L (Rubisco large subunit) were analyzed. The amino acids compositions and grand average of hydropathicity of freshwater <i>H. rivularis</i> and marine <i>H. rubra</i> were similar. Rubisco large subunit of <i>Hildenbrandia</i> was hydrophilic and the secondary structure was primarily composed of α-helixes and β-sheets, revealing the relatively stable structure of this protein. The predicted phosphorylation sites in <i>H. rivularis</i> and <i>H. rubra</i> were 33 and 36, respectively. No positive selection sites were detected in the genus <i>Hildenbrandia</i>, implying that <i>rbc</i>L gene evolved either neutrally or under purifying selection. A total of 41 coevolutionary groups were detected in the Rubisco large subunit of <i>Hildenbrandia</i> and the coevolving sites are in closer proximity in 3-dimensional structure of the protein. Despite the long evolutionary history, <i>rbc</i>L gene in genus <i>Hildenbrandia</i> under different environments is rather conservative.</p>","PeriodicalId":1,"journal":{"name":"Accounts of Chemical Research","volume":null,"pages":null},"PeriodicalIF":16.4000,"publicationDate":"2020-12-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1177/1176934320977862","citationCount":"1","resultStr":"{\"title\":\"Analysis of Adaptive Evolution and Coevolution of <i>rbc</i>L Gene in the Genus <i>Hildenbrandia</i> (Rhodophyta).\",\"authors\":\"Nan Fangru, Han Yuxin, Liu Xudong, Feng Jia, Lv Junping, Liu Qi, Xie Shulian\",\"doi\":\"10.1177/1176934320977862\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The adaptive evolution and coevolution of the ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit (<i>rbc</i>L) gene in the genus <i>Hildenbrandia</i> were studied based on phylogenetic tree construction and the physicochemical properties and the secondary structures of protein encoded by <i>rbc</i>L (Rubisco large subunit) were analyzed. The amino acids compositions and grand average of hydropathicity of freshwater <i>H. rivularis</i> and marine <i>H. rubra</i> were similar. Rubisco large subunit of <i>Hildenbrandia</i> was hydrophilic and the secondary structure was primarily composed of α-helixes and β-sheets, revealing the relatively stable structure of this protein. The predicted phosphorylation sites in <i>H. rivularis</i> and <i>H. rubra</i> were 33 and 36, respectively. No positive selection sites were detected in the genus <i>Hildenbrandia</i>, implying that <i>rbc</i>L gene evolved either neutrally or under purifying selection. A total of 41 coevolutionary groups were detected in the Rubisco large subunit of <i>Hildenbrandia</i> and the coevolving sites are in closer proximity in 3-dimensional structure of the protein. Despite the long evolutionary history, <i>rbc</i>L gene in genus <i>Hildenbrandia</i> under different environments is rather conservative.</p>\",\"PeriodicalId\":1,\"journal\":{\"name\":\"Accounts of Chemical Research\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":16.4000,\"publicationDate\":\"2020-12-16\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1177/1176934320977862\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Accounts of Chemical Research\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1177/1176934320977862\",\"RegionNum\":1,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2020/1/1 0:00:00\",\"PubModel\":\"eCollection\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Accounts of Chemical Research","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1177/1176934320977862","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2020/1/1 0:00:00","PubModel":"eCollection","JCR":"Q1","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
Analysis of Adaptive Evolution and Coevolution of rbcL Gene in the Genus Hildenbrandia (Rhodophyta).
The adaptive evolution and coevolution of the ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit (rbcL) gene in the genus Hildenbrandia were studied based on phylogenetic tree construction and the physicochemical properties and the secondary structures of protein encoded by rbcL (Rubisco large subunit) were analyzed. The amino acids compositions and grand average of hydropathicity of freshwater H. rivularis and marine H. rubra were similar. Rubisco large subunit of Hildenbrandia was hydrophilic and the secondary structure was primarily composed of α-helixes and β-sheets, revealing the relatively stable structure of this protein. The predicted phosphorylation sites in H. rivularis and H. rubra were 33 and 36, respectively. No positive selection sites were detected in the genus Hildenbrandia, implying that rbcL gene evolved either neutrally or under purifying selection. A total of 41 coevolutionary groups were detected in the Rubisco large subunit of Hildenbrandia and the coevolving sites are in closer proximity in 3-dimensional structure of the protein. Despite the long evolutionary history, rbcL gene in genus Hildenbrandia under different environments is rather conservative.
期刊介绍:
Accounts of Chemical Research presents short, concise and critical articles offering easy-to-read overviews of basic research and applications in all areas of chemistry and biochemistry. These short reviews focus on research from the author’s own laboratory and are designed to teach the reader about a research project. In addition, Accounts of Chemical Research publishes commentaries that give an informed opinion on a current research problem. Special Issues online are devoted to a single topic of unusual activity and significance.
Accounts of Chemical Research replaces the traditional article abstract with an article "Conspectus." These entries synopsize the research affording the reader a closer look at the content and significance of an article. Through this provision of a more detailed description of the article contents, the Conspectus enhances the article's discoverability by search engines and the exposure for the research.