[Stoichiometry of GTP hydrolysis during peptide synthesis on the ribosome. I. Factor-independent GTPase and ATPase of ribosomal preparations].
It has been found that preparations of Escherichia coli (MRE-600) ribosomes can display GTPase and ATPase activities independent of elongation factors EF-Tu and EF-G. The GTPase and ATPase are localized on ribosomal 50S subparticles, whereas 30S subparticles are free of the activities and do not stimulate them upon association with the 50S subparticles to form complete ribosomes. The GTPase and ATPase can be removed from the ribosomes and their 50S subparticles by treatment with 1 M NH4Cl or 50% ethanol in the cold. Ribosomal preparations freed from the factor-independent GTPase and ATPase retain their basic functional features. The data obtained do not permit to solve finally whether the factor-independent GTPase and ATPase revealed are components of ribosomes or represent a contamination rather firmly bound to the ribosomes. However, in any case this finding can contribute to an uncoupled hydrolysis of GTP and should be considered when studying the stoichiometry of triphosphate expenditure in the process of ribosomal protein synthesis.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D020963:GTP Phosphohydrolase-Linked Elongation Factors / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism*; D007700:Kinetics; D010445:Peptide Elongation Factors / Q000378:metabolism; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D012270:Ribosomes / Q000201:enzymology*
D010445:Peptide Elongation Factors; D006160:Guanosine Triphosphate; D010744:Phosphoric Monoester Hydrolases; D000251:Adenosine Triphosphatases; D020963:GTP Phosphohydrolase-Linked Elongation Factors
Izuchenie stekhiometrii raspada GTP pri sinteze peptida na ribosome. Faktornezavisimaia GTPaza i ATPaza preparatov ribosom.