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RNA. 2012 May;18(5):886-99. doi: 10.1261/rna.032300.112. Epub 2012 Mar 28.

Doing it in reverse: 3'-to-5' polymerization by the Thg1 superfamily.

Author information

1
Department of Biochemistry and Center for RNA Biology, The Ohio State University, Columbus, Ohio 43210, USA. jackman.14@osu.edu

Abstract

The tRNA(His) guanylyltransferase (Thg1) family of enzymes comprises members from all three domains of life (Eucarya, Bacteria, Archaea). Although the initial activity associated with Thg1 enzymes was a single 3'-to-5' nucleotide addition reaction that specifies tRNA(His) identity in eukaryotes, the discovery of a generalized base pair-dependent 3'-to-5' polymerase reaction greatly expanded the scope of Thg1 family-catalyzed reactions to include tRNA repair and editing activities in bacteria, archaea, and organelles. While the identification of the 3'-to-5' polymerase activity associated with Thg1 enzymes is relatively recent, the roots of this discovery and its likely physiological relevance were described ≈ 30 yr ago. Here we review recent advances toward understanding diverse Thg1 family enzyme functions and mechanisms. We also discuss possible evolutionary origins of Thg1 family-catalyzed 3'-to-5' addition activities and their implications for the currently observed phylogenetic distribution of Thg1-related enzymes in biology.

PMID:
22456265
PMCID:
PMC3334698
DOI:
10.1261/rna.032300.112
[Indexed for MEDLINE]
Free PMC Article

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