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. 1978 Dec;5(12):4865–4876. doi: 10.1093/nar/5.12.4865

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

R D McKinnon, M A Wosnick, B N White
PMCID: PMC342794  PMID: 106366

Abstract

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, tRNA2gammaAsp. The QU-lacking (gamma) 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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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