Open AccessThe Elongation Factor Tu · Guanosine Tetraphosphate Complex
Author(s) -
PINGOUD Alfred,
BLOCK Wolfgang
Publication year - 1981
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1981.tb05382.x
Subject(s) - guanosine , guanosine diphosphate , ef tu , ternary complex , guanosine triphosphate , chemistry , gtpase , escherichia coli , biochemistry , adenosine triphosphate , enzyme , gtp' , transfer rna , rna , gene
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.