FEBS Letters
Volume 582, Issue 15 , Pages 2178-2182, 25 June 2008

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

Edited by Gianni Cesareni

  • Corinne D. Hausmann

      Affiliations

    • Department of Microbiology, The Ohio State University, 484 West 12th Avenue, Columbus, OH 43210-1292, USA
    • ,
  • Michael Ibba

      Affiliations

    • Department of Microbiology, The Ohio State University, 484 West 12th Avenue, Columbus, OH 43210-1292, USA
    • Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210-1292, USA
    • Corresponding Author InformationCorresponding author. Address: Department of Microbiology, The Ohio State University, 484 West 12th Avenue, Columbus, OH 43210-1292, USA. Fax: +1 614 292 8120.

Received 11 May 2008; received in revised form 20 May 2008; accepted 26 May 2008. published online 05 June 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.

Structured summary


MINT-6551032:

EF1A (uniprotkb:O27132) physically interacts (MI:0218) with LeuRS (uniprotkb:O27552) by surface plasmon resonance (MI:0107)

Abbreviation: aaRS, aminoacyl-tRNA synthetase

Keywords: Aminoacyl-tRNA synthetase, Translation, Amino acid

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PII: S0014-5793(08)00473-0

doi:10.1016/j.febslet.2008.05.043

FEBS Letters
Volume 582, Issue 15 , Pages 2178-2182, 25 June 2008

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