title: The elongation factor Tu . guanosine tetraphosphate complex.
abstract: The elongation factor Tu (EF-Tu) isolated from Escherichia coli cells that have undergone the stringent response is predominantly complexed with guanosine 5'-diphosphate 3'-diphosphate. This complex can be separated by anion-exchange chromatography from Ef-Tu . GDP. Unlike EF-Tu complexed with guanosine 5'-triphosphate 3'-diphosphate, the complex with guanosine 5'-diphosphate 3'-diphosphate cannot form a ternary complex with aminoacyl-tRNAs as can be shown directly by hydrolysis protection experiments.
mesh_terms: D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004926:Escherichia coli / Q000201:enzymology; D006150:Guanine Nucleotides / Q000378:metabolism*; D006153:Guanosine Diphosphate / Q000378:metabolism; D006159:Guanosine Tetraphosphate / Q000378:metabolism*; D006868:Hydrolysis; D010444:Peptide Elongation Factor Tu; D010445:Peptide Elongation Factors / Q000302:isolation & purification / Q000378:metabolism*; D011485:Protein Binding; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D006150:Guanine Nucleotides; D010445:Peptide Elongation Factors; D012346:RNA, Transfer, Amino Acyl; D006153:Guanosine Diphosphate; D006159:Guanosine Tetraphosphate; D010444:Peptide Elongation Factor Tu