Open AccessInduced formation of covalent bonds between nucleoprotein components{middle dot} V{middle dot} UV or bisulfite induced polynucleotide-protein crosslinkage in bacteriophage MS2
Author(s) -
E.I. Budowsky,
N.A. Simukova,
M.F. Turchinsky,
Irina V. Boni,
Yu. M. Skoblov
Publication year - 1976
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/3.1.261
Subject(s) - polynucleotide , biology , nucleoprotein , covalent bond , cytosine , nucleic acid , bacteriophage , bisulfite , dna , lysine , deoxyadenosine , biochemistry , rna , amino acid , nucleotide , escherichia coli , stereochemistry , chemistry , organic chemistry , gene expression , gene , dna methylation
UV (lambda = 254 nm) irradiation of bacteriophage MS2 or its treatment with bisulfite induce covalent crosslinkage of the RNA to the coat protein. epilsonN-(2-oxopyrimidyl-4)-lysine was found in the phage hydrolysates after either type of treatment. An equimolar mixture of 0-methylhydroxylamine and bisulfite causes complete disappearance of the cross-links. This led to the conclusion that one of the factors responsible for the UV-induced polynucleotide-protein crosslinkage and the main factor in treatment with bisulfite is substitution of the exocyclic amino group of the activated cytosine nucleus by the lysine residue epilson-amino group of the protein.