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An aminoacyl-tRNA synthetase that specifically activates pyrrolysine
Open accessAbstract
Pyrrolysine, the 22nd cotranslationally inserted amino acid, was found in the Methanosarcina barkeri monomethylamine methyltransferase protein in a position that is encoded by an in-frame UAG stop codon in the mRNA. M. barkeri encodes a special amber suppressor tRNA (tRNA Pyl ) that presumably recognizes this UAG codon. It was reported that Lys-tRNA Pyl can be formed by the aminoacyl-tRNA synthetase-like M. barkeri protein PylS [Srinivasan, G., James, C. M. & Krzycki, J. A. (2002) Science 296, 1459–1462], whereas a later article showed that Lys-tRNA Pyl is synthesized by the combined action of LysRS1 and LysRS2, the two different M. barkeri lysyl-tRNA synthetases. Pyrrolysyl-tRNA Pyl formation was presumed to result from subsequent modification of lysine attached to tRNA Pyl . To investigate whether pyrrolysine can be directly attached to tRNA Pyl we chemically synthesized pyrrolysine. We show that PylS is a specialized aminoacyl-tRNA synthetase for charging pyrrolysine to tRNA Pyl ; lysine and tRNA Lys are not substrates of the enzyme. In view of the properties of PylS we propose to name this enzyme pyrrolysyl-tRNA synthetase. In contrast, the LysRS1:LysRS2 complex does not recognize pyrrolysine and charges tRNA Pyl with lysine. These in vitro data suggest that Methanosarcina cells have two pathways for acylating the suppressor tRNA Pyl . This would ensure efficient translation of the in-frame UAG codon in case of pyrrolysine deficiency and safeguard the biosynthesis of the proteins whose genes contain this special codon.
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Cited by
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Chen, P. R., Groff, D., Guo, J., Ou, W., Cellitti, S., Geierstanger, B. H., & Schultz, P. G. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200900683 · Cited by 269
Genetic code flexibility in microorganisms: novel mechanisms and impact on physiology
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Metadata
- Authors
- Polycarpo, C., Ambrogelly, A., Bérubé, A., Winbush, S. M., McCloskey, J. A., Crain, P. F., Wood, J. L., & Söll, D.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2004-08-16
- Volume
- 101
- Issue
- 34
- Pages
- 12450-12454
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1982826901
- Cited by
- 195
- References
- 0
- FWCI
- 3.72
- Type
- journal article
- Language
- en
- Open access
- green
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- Polycarpo, C., Ambrogelly, A., Bérubé, A., Winbush, S. M., McCloskey, J. A., Crain, P. F., Wood, J. L., & Söll, D. (2004). An aminoacyl-tRNA synthetase that specifically activates pyrrolysine. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0405362101
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