Induced formation of covalent bonds between nucleoprotein components. V. UV or bisulfite induced polynucleotide-protein crosslinkage in bacteriophage MS2.

AUTOR(ES)

Budowsky, E I

RESUMO

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.

Documentos Relacionados

• Mechanism of translational coupling between coat protein and replicase genes of RNA bacteriophage MS2.
• Polynucleotide-protein interactions in the translation system. Identification of proteins interacting with tRNA in the A- and P-sites of E. coli ribosomes.
• Effect of spermidine on the RNA-A protein complex isolated from the RNA bacteriophage MS2.
• Bacteriophage T4 baseplate components. II. Binding and location of bacteriophage-induced dihydrofolate reductase.
• Escherichia coli traD(Ts) mutant temperature sensitive for assembly of RNA bacteriophage MS2.