5' Cap methylation of homologous poly A(+) RNA by a RNA (guanine-7) methyltransferase from Neurospora crassa. |
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Authors: | J Germershausen D Goodman E W Somberg |
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Institution: | Biochemistry Laboratory Department of Zoology and Physiology Rutgers, the State University, Newark, New Jersey 07102 USA |
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Abstract: | RNA (guanine-7) methyltransferase, partially purified from mycelia, catalyzed the transfer of the methyl group from S-adenosylmethionine to the 5′ terminus of both poly A(+) RNA and reovirus unmethylated mRNA. RNase T2 digestion of the methylated poly A(+) RNA from yielded the “cap” structures m 7G(5′)pppAp and m 7G(5′)pppGp in a ratio of 2:1 respectively. RNase T2 digestion of the methylated reovirus mRNA yielded m 7G(5′)pppGp exclusively. The absence of mRNA 2′-0-methyltransferase activity in the enzyme preparation is consistent with the absence of 2′-0-methylation in mRNA Seidel, B. L. and Somberg, E. W. (1978) Arch. Biochem. Biophys. , 108–112]. This is the first isolation of an eucaryotic, cellular RNA (guanine-7) methyltransferase that has been shown to methylate homologous substrate. |
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Keywords: | To whom correspondence should be addressed |
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