Properties of the 5'-terminus of tRNAHis: kinetics of polynucleotide kinase catalyzed exchange and effect of dephosphorylation on the aminoacylation reaction. |
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Authors: | J D Allen S M Parsons |
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Affiliation: | Department of Chemistry, University of California, Santa Barbara, California 93106 USA |
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Abstract: | Bacteriophage T4 induced polynucleotide kinase was found to be ineffective in transferring 32P from [γ-32P]ATP to the 5′-terminus of 5′-phosphorylated tRNAHis using the ADP mediated exchange reaction. However, prior dephosphorylation with alkaline phosphatase allowed polynucleotide kinase catalyzed phosphorylation of tRNAHis. Contrary to reports for other tRNA species, alkaline phosphatase catalyzed 5′-terminus dephosphorylation destroys the amino acid accepting ability of tRNAHis. Aminoacylation competency of the tRNAHis is restored after phosphorylation with polynucleotide kinase. |
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