Aminoacyl-tRNA synthesis in archaea: different but not unique.
Accurate aminoacyl-tRNA synthesis is essential for correct translation of the genetic code in all organisms. Whereas many aspects of this process are conserved, others display a surprisingly high level of divergence from the canonical Escherichia coli model system. These differences are most pronounced in archaea where novel mechanisms have recently been described for aminoacylating tRNAs with asparagine, cysteine, glutamine and lysine. Whereas these mechanisms were initially assumed to be uniquely archaeal, both the alternative asparagine and lysine pathways have subsequently been demonstrated in numerous bacteria. Similarly, studies of the means by which archaea insert the rare amino acid selenocysteine in response to UGA stop codons have helped provide a better understanding of both archaeal and eukaryal selenoprotein synthesis. Most recently a new co-translationally inserted amino acid, pyrrolysine, has been found in archaea although again there is some suggestion that it may also be present in bacteria. Thus, whereas archaea contain a preponderance of non-canonical aminoacyl-tRNA synthesis systems most are also found elsewhere albeit less frequently.
Praetorius-Ibba
Mette
M
Department of Microbiology, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio 43210-1292, USA.
Ibba
Michael
M
D001105:Archaea / Q000235:genetics / Q000378:metabolism*; D003062:Codon; D008239:Lysine / Q000031:analogs & derivatives* / Q000235:genetics / Q000378:metabolism; D008250:Lysine-tRNA Ligase / Q000378:metabolism; D012346:RNA, Transfer, Amino Acyl / Q000096:biosynthesis*; D017279:Selenocysteine / Q000235:genetics / Q000378:metabolism; D014166:Transferases / Q000378:metabolism
D003062:Codon; D012346:RNA, Transfer, Amino Acyl; D017279:Selenocysteine; D014166:Transferases; D008250:Lysine-tRNA Ligase; C456839:pyrrolysine; D008239:Lysine