Distributions of phosphate backbone-produced electrostatic potentials around several tRNAs were calculated by solving the nonlinear Poisson-Boltzmann equation. The tRNAs were either free or bound to the proteins involved in translation: aminoacyl-tRNA and elongation factor EF-Tu. We identified several regions of strong negative potential related to typical structural patterns of tRNA and invariant throughout the tRNAs. The patterns are conserved upon binding of tRNAs to the synthetase and the EF-Tu. Variation of tRNA charge in our theoretical calculations of electrostatic potential-mediated pK shifts of pH-dependent labels attached to tRNA, compared to experimentally observed pK shifts for those labels, shows that the total charge of tRNA is large, within the interval of -40 to -70 proton charges. The electrostatic field of tRNA is sufficient to cause ionization of histidine residues of ARSase, causing additional free energy of ARSase-tRNA interaction of at least several kcal/mol. This may discriminate proteins with respect to the particular tRNA at large distances. Two types of tRNA-protein electrostatic recognition mechanisms are discussed. One, more specific, involves charges induced on protein by the large electrostatic potential of tRNA, while the other, less specific, does not involve induced charges.