AI Article Synopsis
- There is a link between how tRNA modification enzymes recognize multiple tRNA substrates and the presence of heteromultimerization (the combination of different subunits).
- Enzymes that modify the same residue across various tRNA sequences often form a heterodimeric structure to accommodate different substrates while ensuring high specificity in their reactions.
- The review explores two enzyme classes—tRNA methyltransferases and tRNA editing deaminases—focusing on how multimerization may have evolved and its implications for tRNA modifications in various biological systems.
Article 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.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6382703 | PMC |
| http://dx.doi.org/10.3389/fgene.2019.00104 | DOI Listing |
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