{"title":"重组TIS21蛋白精氨酸残基的酶甲基化。","authors":"I K Lim, T J Park, S Kim, H W Lee, W K Paik","doi":"10.1002/iub.7510450504","DOIUrl":null,"url":null,"abstract":"<p><p>Recombinant TIS21 protein was overexpressed in Escherichia coli harboring the expression vector plasmid pQE-30 carrying the TIS21 cDNA coding sequence containing an extra 120 nucleotides upstream. Employing this protein consisting of 158 amino acid residues of the main chain plus 40 residues of the fusion peptide. It was found that one of the protein methylase I group [S-adenosylmethionine:nuclear protein/histone-arginine N-methyltransferase; BC 2.1.1.23; J. Biol. Chem., 269, 1075 (1994)] methylated this protein. The methylation products were identified as guanidino-N-methylated arginines. Some of the kinetics of the reaction are described.</p>","PeriodicalId":8770,"journal":{"name":"Biochemistry and molecular biology international","volume":"45 5","pages":"871-8"},"PeriodicalIF":0.0000,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/iub.7510450504","citationCount":"13","resultStr":"{\"title\":\"Enzymatic methylation of recombinant TIS21 protein-arginine residues.\",\"authors\":\"I K Lim, T J Park, S Kim, H W Lee, W K Paik\",\"doi\":\"10.1002/iub.7510450504\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Recombinant TIS21 protein was overexpressed in Escherichia coli harboring the expression vector plasmid pQE-30 carrying the TIS21 cDNA coding sequence containing an extra 120 nucleotides upstream. Employing this protein consisting of 158 amino acid residues of the main chain plus 40 residues of the fusion peptide. It was found that one of the protein methylase I group [S-adenosylmethionine:nuclear protein/histone-arginine N-methyltransferase; BC 2.1.1.23; J. Biol. Chem., 269, 1075 (1994)] methylated this protein. The methylation products were identified as guanidino-N-methylated arginines. Some of the kinetics of the reaction are described.</p>\",\"PeriodicalId\":8770,\"journal\":{\"name\":\"Biochemistry and molecular biology international\",\"volume\":\"45 5\",\"pages\":\"871-8\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1998-08-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1002/iub.7510450504\",\"citationCount\":\"13\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochemistry and molecular biology international\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1002/iub.7510450504\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochemistry and molecular biology international","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1002/iub.7510450504","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 13
摘要
重组TIS21蛋白在大肠杆菌中过表达,表达载体质粒pQE-30携带TIS21 cDNA编码序列,该序列在上游额外增加120个核苷酸。该蛋白由主链的158个氨基酸残基加上融合肽的40个残基组成。发现其中1组蛋白甲基化酶[s -腺苷蛋氨酸:核蛋白/组蛋白精氨酸n -甲基转移酶;公元前2.1.1.23;生物。化学。[j] .生物工程学报,1999,19(2):1。甲基化产物被鉴定为胍- n -甲基化精氨酸。对反应的一些动力学进行了描述。
Enzymatic methylation of recombinant TIS21 protein-arginine residues.
Recombinant TIS21 protein was overexpressed in Escherichia coli harboring the expression vector plasmid pQE-30 carrying the TIS21 cDNA coding sequence containing an extra 120 nucleotides upstream. Employing this protein consisting of 158 amino acid residues of the main chain plus 40 residues of the fusion peptide. It was found that one of the protein methylase I group [S-adenosylmethionine:nuclear protein/histone-arginine N-methyltransferase; BC 2.1.1.23; J. Biol. Chem., 269, 1075 (1994)] methylated this protein. The methylation products were identified as guanidino-N-methylated arginines. Some of the kinetics of the reaction are described.