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Structural and functional mapping of the archaeal multi-aminoacyl-tRNA synthetase complex.

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.

SUBMITTER: Hausmann CD

PROVIDER: S-EPMC2486338 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature

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Structural and functional mapping of the archaeal multi-aminoacyl-tRNA synthetase complex.

Hausmann Corinne D CD Ibba Michael M

FEBS letters 20080605 15

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 s ...[more]

PMID: 18538672

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