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Linking energy production and protein synthesis in hydrogenotrophic methanogens

Biochemistry. 2012 Mar 27;51(12):2378-89. doi: 10.1021/bi300106p. Epub 2012 Mar 13.

Abstract

Hydrogenotrophic methanogens possessing the hydrogen-dependent dehydrogenase Hmd also encode paralogs of this protein whose function is poorly understood. Here we present biochemical evidence that the two inactive Hmd paralogs of Methanocaldococcus jannaschii, HmdII and HmdIII, form binary and ternary complexes with several components of the protein translation apparatus. HmdII and HmdIII, but not the active dehydrogenase Hmd, bind with micromolar binding affinities to a number of tRNAs and form ternary complexes with tRNA(Pro) and prolyl-tRNA synthetase (ProRS). Fluorescence spectroscopy experiments also suggest that binding of HmdII and ProRS involves distinct binding determinants on the tRNA. These biochemical data suggest the possibility of a regulatory link between energy production and protein translation pathways that may allow a rapid cellular response to altered environmental conditions.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Archaeal Proteins / biosynthesis*
  • Archaeal Proteins / chemistry
  • Archaeal Proteins / metabolism
  • Hydrogen / metabolism*
  • Methanococcaceae / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Multimerization
  • Protein Structure, Quaternary
  • Thermodynamics

Substances

  • Archaeal Proteins
  • Hydrogen