The kinetics of the tRNA cycle is in itself capable of keeping the translational error level almost unaffected by amino acid starvation. There is no need to assume any yet unknown mechanism or property. Kinetic analysis shows that the concentration of aminoacyl-tRNA can stay high even for large reductions in amino-acylation, since the pool of unchanged tRNA normally is very small. An enhanced binding of uncharged tRNA to the ribosome could increase the effect and produce an extremely efficient error damping. A similar result is obtained when EF-Tu is partially inhibited by ppGpp.
