{"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}
引用次数: 37
Abstract
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.
京公网安备 11010802042870号
京ICP备2023020795号-1
分享
求助内容：
应助结果提醒方式：
扫码关注我们
