{"title":"Primary structure of an acidic ribosomal protein YPA1 from Saccharomyces cerevisiae","authors":"Takuzi Itoh","doi":"10.1016/0005-2795(81)90088-X","DOIUrl":null,"url":null,"abstract":"<div><p>The complete primary structure of an acidic ribosomal protein YPA1 from <em>Saccharomyces cerevisiae</em> has been determined. YPA1 is composed of 110 amino acid residues and has the composition: Asp<sub>7</sub>, Asn<sub>2</sub>, Thr<sub>2</sub>, Ser<sub>9</sub>, Glu<sub>15</sub>, Gln<sub>2</sub>, Pro<sub>3</sub>, Gly<sub>15</sub>, Ala<sub>21</sub>, Val<sub>6</sub>, Met<sub>2</sub>, Ile<sub>4</sub>, Leu<sub>9</sub>, Tyr<sub>2</sub>, Phe<sub>3</sub>, Lys<sub>7</sub> and Arg<sub>1</sub>. The molecular weight of YPA1 is 11 020. The amino acid sequence was determined by <span><math><mtext>4-N,N-</mtext><mtext>dimethylaminoazobenzene</mtext></math></span> 4′-isothiocyanate degradation of the peptides obtained by digestions with trypsin, chymotrypsin, thermolysin, pepsin and <em>Staphylococcus aureus</em> protease of intact protein. A comparison of protein YPA1 from yeast with eL12 from <em>Artemia salina</em> shows a high sequence similarity. A considerable similarity is also shown with HL20 from <em>Halobacterium cutirubrum</em>. On the other hand, there is very little apparent sequence similarity between YPA1 and the eubacterial acidic protein L12 either from <em>E. coli</em> or <em>B. subtilis</em>.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1981-11-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90088-X","citationCount":"24","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Protein Structure","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/000527958190088X","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 24
Abstract
The complete primary structure of an acidic ribosomal protein YPA1 from Saccharomyces cerevisiae has been determined. YPA1 is composed of 110 amino acid residues and has the composition: Asp7, Asn2, Thr2, Ser9, Glu15, Gln2, Pro3, Gly15, Ala21, Val6, Met2, Ile4, Leu9, Tyr2, Phe3, Lys7 and Arg1. The molecular weight of YPA1 is 11 020. The amino acid sequence was determined by 4′-isothiocyanate degradation of the peptides obtained by digestions with trypsin, chymotrypsin, thermolysin, pepsin and Staphylococcus aureus protease of intact protein. A comparison of protein YPA1 from yeast with eL12 from Artemia salina shows a high sequence similarity. A considerable similarity is also shown with HL20 from Halobacterium cutirubrum. On the other hand, there is very little apparent sequence similarity between YPA1 and the eubacterial acidic protein L12 either from E. coli or B. subtilis.
已经确定了酿酒酵母酸性核糖体蛋白YPA1的完整一级结构。YPA1由110个氨基酸残基组成,其组成为:Asp7、Asn2、Thr2、Ser9、Glu15、Gln2、Pro3、Gly15、Ala21、Val6、Met2、Ile4、Leu9、Tyr2、Phe3、Lys7和Arg1。YPA1的分子量为11 020。用胰蛋白酶、凝乳胰蛋白酶、热溶酶、胃蛋白酶和金黄色葡萄球菌蛋白酶消化得到的肽段,用4- n, n -二甲氨基偶氮苯4′-异硫氰酸酯降解得到氨基酸序列。酵母中YPA1蛋白与盐渍蒿中eL12蛋白的序列相似性较高。与角质盐杆菌的HL20也有相当大的相似性。另一方面,无论是大肠杆菌还是枯草芽孢杆菌,YPA1与真菌性酸性蛋白L12之间的序列相似性都很小。