| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2050002 | FEBS Letters | 2008 | 5 Pages |
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.Structured summaryMINT-6551032:EF1A (uniprotkb:O27132) physically interacts (MI:0218) with LeuRS (uniprotkb:O27552) by surface plasmon resonance (MI:0107)
