Oleskina YuP, N P Yurina, T I Odintsova, T A Egorov, A Otto, B Wittmann-Liebold, M S Odintsova
{"title":"豌豆叶绿体的核糖体蛋白:检测到一种与核糖体蛋白同源的蛋白。","authors":"Oleskina YuP, N P Yurina, T I Odintsova, T A Egorov, A Otto, B Wittmann-Liebold, M S Odintsova","doi":"10.1080/15216549900201843","DOIUrl":null,"url":null,"abstract":"<p><p>Basic proteins were isolated from purified pea chloroplast nucleoids by acid extraction. Using RP-HPLC, the component composition of the basic proteins was studied. SDS-PAGE of major HPLC-fractions showed that the basic nucleoid proteins are heterogeneous with mol. masses of components from 17 to 30 kDa. One polypeptide with mol. mass of 28 kDa (P28) was obtained by RP-HPLC. The sequencing of three tryptic peptides of P28 (T6, T17, and T19) showed that they are homologous to the ribosomal protein L19 of Saccharomyces cerevisiae. The possible functional role of ribosomal proteins in chloroplast nucleoids is discussed.</p>","PeriodicalId":8770,"journal":{"name":"Biochemistry and molecular biology international","volume":"47 5","pages":"757-63"},"PeriodicalIF":0.0000,"publicationDate":"1999-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/15216549900201843","citationCount":"9","resultStr":"{\"title\":\"Nucleoid proteins of pea chloroplasts: detection of a protein homologous to ribosomal protein.\",\"authors\":\"Oleskina YuP, N P Yurina, T I Odintsova, T A Egorov, A Otto, B Wittmann-Liebold, M S Odintsova\",\"doi\":\"10.1080/15216549900201843\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Basic proteins were isolated from purified pea chloroplast nucleoids by acid extraction. Using RP-HPLC, the component composition of the basic proteins was studied. SDS-PAGE of major HPLC-fractions showed that the basic nucleoid proteins are heterogeneous with mol. masses of components from 17 to 30 kDa. One polypeptide with mol. mass of 28 kDa (P28) was obtained by RP-HPLC. The sequencing of three tryptic peptides of P28 (T6, T17, and T19) showed that they are homologous to the ribosomal protein L19 of Saccharomyces cerevisiae. The possible functional role of ribosomal proteins in chloroplast nucleoids is discussed.</p>\",\"PeriodicalId\":8770,\"journal\":{\"name\":\"Biochemistry and molecular biology international\",\"volume\":\"47 5\",\"pages\":\"757-63\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1999-05-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1080/15216549900201843\",\"citationCount\":\"9\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochemistry and molecular biology international\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1080/15216549900201843\",\"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/10.1080/15216549900201843","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Nucleoid proteins of pea chloroplasts: detection of a protein homologous to ribosomal protein.
Basic proteins were isolated from purified pea chloroplast nucleoids by acid extraction. Using RP-HPLC, the component composition of the basic proteins was studied. SDS-PAGE of major HPLC-fractions showed that the basic nucleoid proteins are heterogeneous with mol. masses of components from 17 to 30 kDa. One polypeptide with mol. mass of 28 kDa (P28) was obtained by RP-HPLC. The sequencing of three tryptic peptides of P28 (T6, T17, and T19) showed that they are homologous to the ribosomal protein L19 of Saccharomyces cerevisiae. The possible functional role of ribosomal proteins in chloroplast nucleoids is discussed.