Juan Lin, Wen Zhang, Mingzhu Shi, Xinglong Wang, Xiaofen Sun, K. Tang
{"title":"法氏囊荠菜cax基因的分离及分子特征分析。","authors":"Juan Lin, Wen Zhang, Mingzhu Shi, Xinglong Wang, Xiaofen Sun, K. Tang","doi":"10.32604/BIOCELL.2008.32.229","DOIUrl":null,"url":null,"abstract":"A new cation exchangers (CAXs) gene was cloned and characterized from Capsella bursa-pastoris by rapid amplification of cDNA ends (RACE). The full-length cDNA sequence of cax from C. bursa-pastoris (designated as Cbcax51) was 1754 bp containing a 1398 bp open reading frame encoding a polypeptide of 466 amino-acid residues with a calculated molecular mass of 50.5 kDa and an isoelectric point of 5.69. The predicted CbCAX51 contained an IMP dehydrogenase/GMP reductase domain, two Na+/Ca2+ exchanger protein domains. Comparative and bioinformatics analyses revealed that CbCAX51 showed extensive homology with CAX from other plant species. The expression analysis by different treatments indicated that Cbcax51 could be activated by cold triggering and was related to the cold acclimation process, but its expression is regulated negatively by drought and not affected by ABA or salt.","PeriodicalId":342778,"journal":{"name":"Biocell : official journal of the Sociedades Latinoamericanas de Microscopia Electronica ... et. al","volume":"2015 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2008-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"6","resultStr":"{\"title\":\"Isolation and molecular characterization of a cax gene from Capsella bursa-pastoris.\",\"authors\":\"Juan Lin, Wen Zhang, Mingzhu Shi, Xinglong Wang, Xiaofen Sun, K. Tang\",\"doi\":\"10.32604/BIOCELL.2008.32.229\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"A new cation exchangers (CAXs) gene was cloned and characterized from Capsella bursa-pastoris by rapid amplification of cDNA ends (RACE). The full-length cDNA sequence of cax from C. bursa-pastoris (designated as Cbcax51) was 1754 bp containing a 1398 bp open reading frame encoding a polypeptide of 466 amino-acid residues with a calculated molecular mass of 50.5 kDa and an isoelectric point of 5.69. The predicted CbCAX51 contained an IMP dehydrogenase/GMP reductase domain, two Na+/Ca2+ exchanger protein domains. Comparative and bioinformatics analyses revealed that CbCAX51 showed extensive homology with CAX from other plant species. The expression analysis by different treatments indicated that Cbcax51 could be activated by cold triggering and was related to the cold acclimation process, but its expression is regulated negatively by drought and not affected by ABA or salt.\",\"PeriodicalId\":342778,\"journal\":{\"name\":\"Biocell : official journal of the Sociedades Latinoamericanas de Microscopia Electronica ... et. al\",\"volume\":\"2015 1\",\"pages\":\"0\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2008-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"6\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biocell : official journal of the Sociedades Latinoamericanas de Microscopia Electronica ... et. al\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.32604/BIOCELL.2008.32.229\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biocell : official journal of the Sociedades Latinoamericanas de Microscopia Electronica ... et. al","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.32604/BIOCELL.2008.32.229","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Isolation and molecular characterization of a cax gene from Capsella bursa-pastoris.
A new cation exchangers (CAXs) gene was cloned and characterized from Capsella bursa-pastoris by rapid amplification of cDNA ends (RACE). The full-length cDNA sequence of cax from C. bursa-pastoris (designated as Cbcax51) was 1754 bp containing a 1398 bp open reading frame encoding a polypeptide of 466 amino-acid residues with a calculated molecular mass of 50.5 kDa and an isoelectric point of 5.69. The predicted CbCAX51 contained an IMP dehydrogenase/GMP reductase domain, two Na+/Ca2+ exchanger protein domains. Comparative and bioinformatics analyses revealed that CbCAX51 showed extensive homology with CAX from other plant species. The expression analysis by different treatments indicated that Cbcax51 could be activated by cold triggering and was related to the cold acclimation process, but its expression is regulated negatively by drought and not affected by ABA or salt.