Elongation factors in protein synthesis.
Recent discoveries of elongation factor-related proteins have considerably complicated the simple textbook scheme of the peptide chain elongation cycle. During growth and differentiation the cycle may be regulated not only by factor modification but also factor replacement. In addition, rare tRNAs may have their own rare factor proteins. A special case is the acquisition of resistance by bacteria to elongation factor-directed antibiotics. Pertinent data from the literature and our own work with Escherichia coli and Streptomyces are discussed. The GTP-binding domain of EF-Tu has been studied extensively, but little molecular detail is available on the interactions with its other ligands or effectors, or on the way they are affected by the GTPase switch signal. A growing number of EF-Tu mutants obtained by ourselves and others are helping us in testing current ideas. We have found a synergistic effect between EF-Tu and EF-G in their uncoupled GTPase reactions on empty ribosomes. Only the EF-G reaction is perturbed by fluoroaluminates.
Kraal
B
B
Department of Biochemistry, Leiden University, The Netherlands.
Bosch
L
L
Mesters
J R
JR
de Graaf
J M
JM
Woudt
L P
LP
Vijgenboom
E
E
Heinstra
P W
PW
Zeef
L A
LA
Boon
C
C
D000818:Animals; D016296:Mutagenesis / Q000502:physiology; D010445:Peptide Elongation Factors / Q000737:chemistry / Q000502:physiology*; D014176:Protein Biosynthesis; D011487:Protein Conformation; D012270:Ribosomes / Q000502:physiology; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
D010445:Peptide Elongation Factors