The site for GTP hydrolysis on the archaeal elongation factor 2 is unmasked by aliphatic alcohols

Biochimie. 1996;78(10):832-7. doi: 10.1016/s0300-9084(97)84335-0.

Abstract

An appropriate mixture of ethylene glycol and BaCl2 enhanced the otherwise very low intrinsic GTPase activity of the elongation factor 2 isolated from the archaeon Sulfolobus solfataricus (SsEF-2). The enzymatic activity became up to 300-fold higher than that of the SsEF-2 GTPase measured in the absence of any stimulator, but remained 20-fold lower than that stimulated by ribosome. The stimulatory effect of ethylene glycol/Ba2+ was attributed to the increased affinity for GTP, probably related to a conformational change occurring in a hydrophobic region near the catalytic site.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate Ribose
  • Alcohols / pharmacology*
  • Barium Compounds / pharmacology
  • Binding Sites
  • Cations, Divalent / pharmacology
  • Chlorides / pharmacology
  • Ethylene Glycol
  • Ethylene Glycols / pharmacology
  • GTP Phosphohydrolase-Linked Elongation Factors / metabolism
  • GTP-Binding Proteins / metabolism
  • Guanosine Diphosphate / pharmacology
  • Guanosine Triphosphate / metabolism*
  • Guanosine Triphosphate / pharmacology
  • Guanylyl Imidodiphosphate / metabolism
  • Guanylyl Imidodiphosphate / pharmacology
  • Hydrogen-Ion Concentration
  • Hydrolysis
  • Peptide Elongation Factor 2
  • Peptide Elongation Factors / drug effects
  • Peptide Elongation Factors / metabolism*
  • Sulfolobus / enzymology*
  • Temperature

Substances

  • Alcohols
  • Barium Compounds
  • Cations, Divalent
  • Chlorides
  • Ethylene Glycols
  • Peptide Elongation Factor 2
  • Peptide Elongation Factors
  • barium chloride
  • Guanosine Diphosphate
  • Adenosine Diphosphate Ribose
  • Guanylyl Imidodiphosphate
  • Guanosine Triphosphate
  • GTP Phosphohydrolase-Linked Elongation Factors
  • GTP-Binding Proteins
  • Ethylene Glycol