|Title||One polypeptide with two aminoacyl-tRNA synthetase activities.|
|Publication Type||Journal Article|
|Year of Publication||2000|
|Authors||Stathopoulos C, Li T, Longman R, Vothknecht UC, Becker HD, Ibba M, Söll D|
|Date Published||2000 Jan 21|
|Keywords||Amino Acyl-tRNA Synthetases, Binding Sites, Cysteine, Escherichia coli, Evolution, Molecular, Genes, Archaeal, Methanococcus, Multienzyme Complexes, Proline, RNA, Transfer, Amino Acyl, Sequence Analysis, Protein, Substrate Specificity, Transfer RNA Aminoacylation, Transformation, Bacterial|
The genome sequences of certain archaea do not contain recognizable cysteinyl-transfer RNA (tRNA) synthetases, which are essential for messenger RNA-encoded protein synthesis. However, a single cysteinyl-tRNA synthetase activity was detected and purified from one such organism, Methanococcus jannaschii. The amino-terminal sequence of this protein corresponded to the predicted sequence of prolyl-tRNA synthetase. Biochemical and genetic analyses indicated that this archaeal form of prolyl-tRNA synthetase can synthesize both cysteinyl-tRNA(Cys) and prolyl-tRNA(Pro). The ability of one enzyme to provide two aminoacyl-tRNAs for protein synthesis raises questions about concepts of substrate specificity in protein synthesis and may provide insights into the evolutionary origins of this process.
Pfizer COVID-19 vaccine appointments are available to our patients. Sign up for Connect today to schedule your vaccination.