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Front Genet. 2019 Feb 14;10:104. doi: 10.3389/fgene.2019.00104. eCollection 2019.

Multi-Substrate Specificity and the Evolutionary Basis for Interdependence in tRNA Editing and Methylation Enzymes.

Frontiers in genetics

Sameer Dixit, Jeremy C Henderson, Juan D Alfonzo

Affiliations

  1. Department of Microbiology, The Ohio State Biochemistry Program, The Center for RNA Biology, The Ohio State University, Columbus, OH, United States.

PMID: 30838029 PMCID: PMC6382703 DOI: 10.3389/fgene.2019.00104

Abstract

Among tRNA modification enzymes there is a correlation between specificity for multiple tRNA substrates and heteromultimerization. In general, enzymes that modify a conserved residue in different tRNA sequences adopt a heterodimeric structure. Presumably, such changes in the oligomeric state of enzymes, to gain multi-substrate recognition, are driven by the need to accommodate and catalyze a particular reaction in different substrates while maintaining high specificity. This review focuses on two classes of enzymes where the case for multimerization as a way to diversify molecular recognition can be made. We will highlight several new themes with tRNA methyltransferases and will also discuss recent findings with tRNA editing deaminases. These topics will be discussed in the context of several mechanisms by which heterodimerization may have been achieved during evolution and how these mechanisms might impact modifications in different systems.

Keywords: deaminase; inosine; methylation; mitochondria; tRNA modification; translation

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