Document Type
Article
Publication Date
6-5-2008
Abstract
Methanothermobacter thermautotrophicus contains a multi-aminoacyl-tRNA synthetase complex (MSC) of LysRS, LeuRS and ProRS. Elongation factor (EF) 1A also associates to the MSC, with LeuRS possibly acting as a core protein. Analysis of the MSC revealed that LysRS and ProRS specifically interact with the idiosyncratic N- and C- termini of LeuRS, respectively. EF-1A instead interacts with the inserted CP1 proofreading domain, consistent with models for post-transfer editing by class I synthetases such as LeuRS. Together with previous genetic data, these findings show that LeuRS plays a central role in mediating interactions within the archaeal MSC by acting as a core scaffolding protein.
Recommended Citation
Hausmann, C.D. and Ibba, M. (2008) Structural and functional mapping of the archaeal multi-aminoacyl-tRNA synthetase complex. FEBS Letts. 582, 2178-2182. https://doi.org10.1016/j.febslet.2008.05.043
Copyright
Federation of European Biochemical Societies
Included in
Amino Acids, Peptides, and Proteins Commons, Biochemistry Commons, Cellular and Molecular Physiology Commons, Molecular Biology Commons, Nucleic Acids, Nucleotides, and Nucleosides Commons, Other Biochemistry, Biophysics, and Structural Biology Commons
Comments
This is a pre-copy-editing, author-produced PDF of an article accepted for publication in FEBS Letters, volume 582, in 2008 following peer review. The definitive publisher-authenticated version is available online at https://doi.org/10.1016/j.febslet.2008.05.043.