ATPase and GTPase activities associated with the 5-S RNA-protein complex of Escherichia coli ribosomes.
Specific 5-S RNA-protein complexes were reconstituted from Escherichia coli 5-S RNA and 50-S ribosomal proteins. These complexes consist of 5-S RNA and two major proteins, namely E-L18 and E-L25. Analysis for enzymatic activities shows that ATP and GTP are hydrolyzed and that this hydrolysis is independent of elongation factors.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D001426:Bacterial Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D020558:GTP Phosphohydrolases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007700:Kinetics; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D012335:RNA, Ribosomal / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000378:metabolism; D012270:Ribosomes / Q000201:enzymology*; D013696:Temperature; D013997:Time Factors
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D012335:RNA, Ribosomal; D012269:Ribosomal Proteins; D010744:Phosphoric Monoester Hydrolases; D000251:Adenosine Triphosphatases; D020558:GTP Phosphohydrolases