Aminoacyl-tRNA synthetases from Haloarcula marismortui: an evidence for a multienzyme complex in a procaryotic system.
Aminoacyl-tRNA synthetases in halophilic archaebacterium Haloarcula marismortui form a high molecular weight multienzyme complex which is resistant to dissociation when subjected to gel filtration, ion exchange, ammonium sulfate mediated and hydroxyapatite chromatography. Functional and structural aspects of the aminoacyl-tRNA synthetase complex formation are discussed.
Goldgur
Y
Y
Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Safro
M
M
D000604:Amino Acyl-tRNA Synthetases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006216:Halobacteriaceae / Q000201:enzymology*; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000378:metabolism*
D009097:Multienzyme Complexes; D000604:Amino Acyl-tRNA Synthetases