Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation.
The three genes, gatC, gatA, and gatB, which constitute the transcriptional unit of the Bacillus subtilis glutamyl-tRNAGln amidotransferase have been cloned. Expression of this transcriptional unit results in the production of a heterotrimeric protein that has been purified to homogeneity. The enzyme furnishes a means for formation of correctly charged Gln-tRNAGln through the transamidation of misacylated Glu-tRNAGln, functionally replacing the lack of glutaminyl-tRNA synthetase activity in Gram-positive eubacteria, cyanobacteria, Archaea, and organelles. Disruption of this operon is lethal. This demonstrates that transamidation is the only pathway to Gln-tRNAGln in B. subtilis and that glutamyl-tRNAGln amidotransferase is a novel and essential component of the translational apparatus.
Curnow
A W
AW
Department of Molecular Biophysics, Yale University, New Haven, CT 06520-8114, USA.
Hong
K w
Kw
Yuan
R
R
Kim
S i
Si
Martins
O
O
Winkler
W
W
Henkin
T M
TM
Söll
D
D
D000215:Acylation; D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology / Q000235:genetics*; D001483:Base Sequence; D003062:Codon; D004926:Escherichia coli / Q000235:genetics; D005973:Glutamine / Q000235:genetics*; D008969:Molecular Sequence Data; D016254:Mutagenesis, Insertional; D019884:Nitrogenous Group Transferases / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D014176:Protein Biosynthesis; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D003062:Codon; D011994:Recombinant Proteins; D005973:Glutamine; D019884:Nitrogenous Group Transferases; C047694:glutamyl-tRNA(Gln) amidotransferase