Specific binding of leucyl transfer RNA to an immature form of L-threonine deaminase: its implications in repression.
The in vitro assembly of L-threonine deaminase from its constituent parts results in the formation of an inactive species of this enzyme which specifically and reversibly binds leucyl-tRNA. The native, catalytically active enzyme, which is derived from this species in the presence of maturation-inducing ligands, does not bind tRNA. The possible involvement of this protein-tRNA complex in the repression of the ilv (ADE) operon is discussed.
D002247:Carbon Isotopes; D006836:Hydro-Lyases / Q000378:metabolism*; D009876:Operon; D011485:Protein Binding; D012343:RNA, Transfer / Q000378:metabolism*; D012486:Salmonella typhimurium / Q000201:enzymology*; D013912:Threonine
D002247:Carbon Isotopes; D013912:Threonine; D012343:RNA, Transfer; D006836:Hydro-Lyases