Structural and functional mapping of the archaeal multi-aminoacyl-tRNA synthetase complex.
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.
Department of Microbiology, The Ohio State University, 484 West 12th Avenue, Columbus, OH 43210-1292, USA.
Corinne D
CD
Hausmann
Michael
M
Ibba
D000604:Amino Acyl-tRNA Synthetases / Q000737:chemistry / Q000378:metabolism; D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism*; D007935:Leucine-tRNA Ligase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008250:Lysine-tRNA Ligase / Q000737:chemistry / Q000378:metabolism; D017013:Methanobacteriaceae / Q000201:enzymology*; D009097:Multienzyme Complexes / Q000737:chemistry / Q000378:metabolism*; D020648:Peptide Elongation Factor 1 / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation
D019843:Archaeal Proteins; D009097:Multienzyme Complexes; D020648:Peptide Elongation Factor 1; D000604:Amino Acyl-tRNA Synthetases; C100134:prolyl T RNA synthetase; D007935:Leucine-tRNA Ligase; D008250:Lysine-tRNA Ligase