Human mitochondrial TyrRS disobeys the tyrosine identity rules.
Human tyrosyl-tRNA synthetase from mitochondria (mt- TyrRS) presents dual sequence features characteristic of eubacterial and archaeal TyrRSs, especially in the region containing amino acids recognizing the N1-N72 tyrosine identity pair. This would imply that human mt- TyrRS has lost the capacity to discriminate between the G1-C72 pair typical of eubacterial and mitochondrial tRNATyr and the reverse pair C1- G72 present in archaeal and eukaryal tRNATyr. This expectation was verified by a functional analysis of wild-type or mutated tRNATyr molecules, showing that mt- TyrRS aminoacylates with similar catalytic efficiency its cognate tRNATyr with G1-C72 and its mutated version with C1- G72. This provides the first example of a TyrRS lacking specificity toward N1-N72 and thus of a TyrRS disobeying the identity rules. Sequence comparisons of mt-TyrRSs across phylogeny suggest that the functional behavior of the human mt- TyrRS is conserved among all vertebrate mt-TyrRSs.[1]References
- Human mitochondrial TyrRS disobeys the tyrosine identity rules. Bonnefond, L., Frugier, M., Giegé, R., Rudinger-Thirion, J. RNA (2005) [Pubmed]
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