L. Alberghina et M. Lotti, THE EVOLUTION OF A NON UNIVERSAL CODON AS DETECTED IN CANDIDA-RUGOSA LIPASE, Journal of molecular catalysis. B, Enzymatic, 3(1-4), 1997, pp. 37-41
In several Candicia species belonging to the same monophyletic group,
CUG - one of the six triplets coding leucine in the universal genetic
code - is read as an additional codon for serine. CUG for serine is ra
rely employed but in the lipase genes of Candida rugosa, where it is t
he major serine codon. This yeast secretes multiple lipase isoenzymes
(CRLs) tightly related in their amino acid sequence. CRL proteins cont
ain 16 to 19 CUG-serines comprehensive of Ser 209 in the catalytic cen
ter and other serines having an obvious structural role. In this paper
, results obtained from sequence analysis and mutagenesis are discusse
d and shown to be consistent with an evolutionary pathway in which the
codon was reassigned via ambiguous decoding by a novel seryl-tRNA who
se abundance conferred positive selection pressure for the extensive u
se of CUG as a serine codon.