| 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 |
| Journal | Science |
| Volume | 287 |
| Issue | 5452 |
| Pagination | 479-82 |
| Date Published | 2000 Jan 21 |
| ISSN | 0036-8075 |
| 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 |
| Abstract | 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. |
| Alternate Journal | Science |
| PubMed ID | 10642548 |