Kiichi Aizawa , Yusuke Saga , Mika Waida , Hiromi Mutsuro-Aoki , Takuya Umehara , Koji Tamura
{"title":"活化核酶KK13的氨基酸的结构还原","authors":"Kiichi Aizawa , Yusuke Saga , Mika Waida , Hiromi Mutsuro-Aoki , Takuya Umehara , Koji Tamura","doi":"10.1016/j.biosystems.2025.105530","DOIUrl":null,"url":null,"abstract":"<div><div>Protein synthesis requires at least three steps: amino acid activation, amino acid transfer to tRNA, and peptide bond formation. Of these, the energy level of the reaction product in the first step, catalyzed by aminoacyl-tRNA synthetase, is the highest, and this reaction consumes ATP and connects amino acids to AMP via acyl phosphate bonds (formation of aminoacyl-AMP). In this study, we focused on KK13, a ribozyme with a length of 114 nucleotides, which catalyzes the formation of acyl phosphate bonds between the α-phosphate of 5ʹ-terminal triphosphate of the ribozyme and the carboxylate of amino acid with concomitant release of inorganic pyrophosphate. Based on the prediction of the secondary and tertiary structures of KK13, we aimed to reduce the size of the ribozyme, plausible on the primitive Earth, which can activate amino acids. Finally, several mutants were created, and the relationship between their structural and evolutionary features is discussed.</div></div>","PeriodicalId":50730,"journal":{"name":"Biosystems","volume":"254 ","pages":"Article 105530"},"PeriodicalIF":1.9000,"publicationDate":"2025-07-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Structural reduction of amino acid activating ribozyme KK13\",\"authors\":\"Kiichi Aizawa , Yusuke Saga , Mika Waida , Hiromi Mutsuro-Aoki , Takuya Umehara , Koji Tamura\",\"doi\":\"10.1016/j.biosystems.2025.105530\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>Protein synthesis requires at least three steps: amino acid activation, amino acid transfer to tRNA, and peptide bond formation. Of these, the energy level of the reaction product in the first step, catalyzed by aminoacyl-tRNA synthetase, is the highest, and this reaction consumes ATP and connects amino acids to AMP via acyl phosphate bonds (formation of aminoacyl-AMP). In this study, we focused on KK13, a ribozyme with a length of 114 nucleotides, which catalyzes the formation of acyl phosphate bonds between the α-phosphate of 5ʹ-terminal triphosphate of the ribozyme and the carboxylate of amino acid with concomitant release of inorganic pyrophosphate. Based on the prediction of the secondary and tertiary structures of KK13, we aimed to reduce the size of the ribozyme, plausible on the primitive Earth, which can activate amino acids. Finally, several mutants were created, and the relationship between their structural and evolutionary features is discussed.</div></div>\",\"PeriodicalId\":50730,\"journal\":{\"name\":\"Biosystems\",\"volume\":\"254 \",\"pages\":\"Article 105530\"},\"PeriodicalIF\":1.9000,\"publicationDate\":\"2025-07-05\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biosystems\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0303264725001406\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biosystems","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0303264725001406","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOLOGY","Score":null,"Total":0}
Structural reduction of amino acid activating ribozyme KK13
Protein synthesis requires at least three steps: amino acid activation, amino acid transfer to tRNA, and peptide bond formation. Of these, the energy level of the reaction product in the first step, catalyzed by aminoacyl-tRNA synthetase, is the highest, and this reaction consumes ATP and connects amino acids to AMP via acyl phosphate bonds (formation of aminoacyl-AMP). In this study, we focused on KK13, a ribozyme with a length of 114 nucleotides, which catalyzes the formation of acyl phosphate bonds between the α-phosphate of 5ʹ-terminal triphosphate of the ribozyme and the carboxylate of amino acid with concomitant release of inorganic pyrophosphate. Based on the prediction of the secondary and tertiary structures of KK13, we aimed to reduce the size of the ribozyme, plausible on the primitive Earth, which can activate amino acids. Finally, several mutants were created, and the relationship between their structural and evolutionary features is discussed.
期刊介绍:
BioSystems encourages experimental, computational, and theoretical articles that link biology, evolutionary thinking, and the information processing sciences. The link areas form a circle that encompasses the fundamental nature of biological information processing, computational modeling of complex biological systems, evolutionary models of computation, the application of biological principles to the design of novel computing systems, and the use of biomolecular materials to synthesize artificial systems that capture essential principles of natural biological information processing.