TY - JOUR
T1 - Glu-tRNAGln amidotransferase
T2 - A novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation
AU - Curnow, Alan W.
AU - Hong, Kwang Won
AU - Yuan, Robert
AU - Kim, Sung Il
AU - Martins, Orlando
AU - Winkler, Wade
AU - Henkin, Tina M.
AU - Söll, Dieter
PY - 1997/10/28
Y1 - 1997/10/28
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0030613553&partnerID=8YFLogxK
U2 - 10.1073/pnas.94.22.11819
DO - 10.1073/pnas.94.22.11819
M3 - Article
C2 - 9342321
AN - SCOPUS:0030613553
SN - 0027-8424
VL - 94
SP - 11819
EP - 11826
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 22
ER -