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Nucleic Acids Research, 1978, Vol. 5, No. 12 4865-4876
© 1978

Articles

The role of the guanine insertion enzyme in Q-biosynthesis in Drosophila melanogaster

Randy D. McKinnon*, Michael A. Wosnick** and Bradley N. White**

The Group in Eukaryotic Molecular Biology and Evolution, Department of Biology, Queen's University Kingston, Ontario, Canada

Received September 13, 1978.

Drosophila tRNA can be guanylated by a crude enzyme from rabbit reticulocytes. Guanylating activity is also present in crude extracts of adult Drosophila A major product of this reaction as well as several minor ones were resolved by RPC-5 chromatography. The main substrate of both the Drosophila and rabbit reticulocyte enzymes was the non-Q-containing aspartic acid tRNA, tRNAAsp. The Q-lacking (y) forms of asparagine, histidine and tyrosine tRNAs were also substrates and gave rise to the minor products of the reaction. In contrast, the Q- or Q*-containing ({delta}) forms of these tRNAs appear not to be substrates. The evidence strongly suggests that the guanyating enzyme is involved in Q biosynthesis and would be better termed a guanine replacement or pre-Q insertion enzyme.

* Present Address: Department of Biology, McMaster University, Hamilton, Ontario, Canada

** Present Address: Division of Medical Biochemistry, Faculty of Medicine University of Calgary, Calgary, Alberta, Canada


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