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pubmed:abstractText |
An enzymic procedure was used to remove the 7-methylguanosine diphosphate moiety at the 5' ends of rabbit hemoglobin mRNA and mouse immunoglobulin light-chain mRNA. Evidence was obtained that the procedure, which involves the use of polynucleotide kinase, does not result in any further degradation of the mRNA. The enzymically decapped mRNA was as effective as untreated mRNA in supporting protein synthesis in a wheat germ system. This was the case over a wide range of mRNA concentrations and over a considerable period of time. The presence in the incubation mixture of S-adenosylhomocysteine, an inhibitor of methylation, did not affect the results. The data indicate that the presence of a 7-methylguanosine diphosphate residue at the 5' end of mRNAs is not an obligatory requirement for translation in eucaryotic systems.
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