C S Jone, N Kotani, K Aso, L Yang, I Enami, K Kondo, A Tsugita
{"title":"嗜热蓝藻长聚球菌光系统I反应中心复合体中8kda蛋白的氨基酸序列。","authors":"C S Jone, N Kotani, K Aso, L Yang, I Enami, K Kondo, A Tsugita","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The 8-kDa protein in Photosystem I (PS I) reaction center complex was isolated from a thermophilic cyanobacterium, Synechococcus elongatus, by SDS-polyacrylamide gel electrophoresis using TRIS-Tricine buffer system. The complete amino acid sequence of the protein was determined. The 8-kDa protein consisted of 73 amino acid residues giving a calculated molecular weight of 7,472. No significant sequence homology were observed with the known other small subunits in PS I reaction center complex, except for the 6.5-kDa protein in PS I from another thermophilic cyanobacterium, S. vulcanus. The 8-kDa protein was characteristically rich in hydrophobic amino acid residues, especially the content of leucine. These suggest that the 8-kDa subunit is an intrinsic structure component in PS I core complex for stabilization of the reaction center.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"4 6","pages":"327-31"},"PeriodicalIF":0.0000,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Amino acid sequence of the 8-kDa protein in photosystem I reaction center complex from a thermophilic cyanobacterium, Synechococcus elongatus.\",\"authors\":\"C S Jone, N Kotani, K Aso, L Yang, I Enami, K Kondo, A Tsugita\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The 8-kDa protein in Photosystem I (PS I) reaction center complex was isolated from a thermophilic cyanobacterium, Synechococcus elongatus, by SDS-polyacrylamide gel electrophoresis using TRIS-Tricine buffer system. The complete amino acid sequence of the protein was determined. The 8-kDa protein consisted of 73 amino acid residues giving a calculated molecular weight of 7,472. No significant sequence homology were observed with the known other small subunits in PS I reaction center complex, except for the 6.5-kDa protein in PS I from another thermophilic cyanobacterium, S. vulcanus. The 8-kDa protein was characteristically rich in hydrophobic amino acid residues, especially the content of leucine. These suggest that the 8-kDa subunit is an intrinsic structure component in PS I core complex for stabilization of the reaction center.</p>\",\"PeriodicalId\":77336,\"journal\":{\"name\":\"Protein sequences & data analysis\",\"volume\":\"4 6\",\"pages\":\"327-31\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1991-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Protein sequences & data analysis\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Protein sequences & data analysis","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Amino acid sequence of the 8-kDa protein in photosystem I reaction center complex from a thermophilic cyanobacterium, Synechococcus elongatus.
The 8-kDa protein in Photosystem I (PS I) reaction center complex was isolated from a thermophilic cyanobacterium, Synechococcus elongatus, by SDS-polyacrylamide gel electrophoresis using TRIS-Tricine buffer system. The complete amino acid sequence of the protein was determined. The 8-kDa protein consisted of 73 amino acid residues giving a calculated molecular weight of 7,472. No significant sequence homology were observed with the known other small subunits in PS I reaction center complex, except for the 6.5-kDa protein in PS I from another thermophilic cyanobacterium, S. vulcanus. The 8-kDa protein was characteristically rich in hydrophobic amino acid residues, especially the content of leucine. These suggest that the 8-kDa subunit is an intrinsic structure component in PS I core complex for stabilization of the reaction center.