{"title":"DNA-组蛋白相互作用对体外DNA生物合成的影响","authors":"Lubomir S. Hnilica, Daniel Billen","doi":"10.1016/0926-6550(64)90251-8","DOIUrl":null,"url":null,"abstract":"<div><p>Calf-thymus histone fractions were found to inhibit the biosynthesis of DNA <em>in vitro</em> to a substantial extent. The inhibition could be explained on the basis of DNA-histone interaction. The very lysine-rich histones (Fraction 1) complexed with DNA most readily and inhibited the DNA replication at a histone-DNA ratio of 1:1 and higher. Higher ratios of the moderately lysine-rich histones (Fraction 2b) and of the arginine-rich histones (Fractions 2a and 3) were required. Complete inhibition was observed only at ratios of histone-DNA of 2:1 and higher. Histone stabilizes the helical molecule of DNA towards heat denaturation. Melting temperatures of reconstituted nucleohistones were determined. Most resistant to the heat denaturation were nucleohistones with a high content of lysine whereas the arginine-rich nucleohistones showed melting temperatures close to those of the DNA.</p></div>","PeriodicalId":100173,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects","volume":"91 2","pages":"Pages 271-280"},"PeriodicalIF":0.0000,"publicationDate":"1964-10-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6550(64)90251-8","citationCount":"37","resultStr":"{\"title\":\"The effect of DNA-histone interactions on the biosynthesis of DNA in vitro\",\"authors\":\"Lubomir S. Hnilica, Daniel Billen\",\"doi\":\"10.1016/0926-6550(64)90251-8\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Calf-thymus histone fractions were found to inhibit the biosynthesis of DNA <em>in vitro</em> to a substantial extent. The inhibition could be explained on the basis of DNA-histone interaction. The very lysine-rich histones (Fraction 1) complexed with DNA most readily and inhibited the DNA replication at a histone-DNA ratio of 1:1 and higher. Higher ratios of the moderately lysine-rich histones (Fraction 2b) and of the arginine-rich histones (Fractions 2a and 3) were required. Complete inhibition was observed only at ratios of histone-DNA of 2:1 and higher. Histone stabilizes the helical molecule of DNA towards heat denaturation. Melting temperatures of reconstituted nucleohistones were determined. Most resistant to the heat denaturation were nucleohistones with a high content of lysine whereas the arginine-rich nucleohistones showed melting temperatures close to those of the DNA.</p></div>\",\"PeriodicalId\":100173,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects\",\"volume\":\"91 2\",\"pages\":\"Pages 271-280\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1964-10-16\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6550(64)90251-8\",\"citationCount\":\"37\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0926655064902518\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926655064902518","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The effect of DNA-histone interactions on the biosynthesis of DNA in vitro
Calf-thymus histone fractions were found to inhibit the biosynthesis of DNA in vitro to a substantial extent. The inhibition could be explained on the basis of DNA-histone interaction. The very lysine-rich histones (Fraction 1) complexed with DNA most readily and inhibited the DNA replication at a histone-DNA ratio of 1:1 and higher. Higher ratios of the moderately lysine-rich histones (Fraction 2b) and of the arginine-rich histones (Fractions 2a and 3) were required. Complete inhibition was observed only at ratios of histone-DNA of 2:1 and higher. Histone stabilizes the helical molecule of DNA towards heat denaturation. Melting temperatures of reconstituted nucleohistones were determined. Most resistant to the heat denaturation were nucleohistones with a high content of lysine whereas the arginine-rich nucleohistones showed melting temperatures close to those of the DNA.
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