Elongation factors in protein synthesis

• Published in: Ciba Foundation symposium Vol. 176; p. 28
• Main Authors: Kraal, B, Bosch, L, Mesters, J R, de Graaf, J M, Woudt, L P, Vijgenboom, E, Heinstra, P W, Zeef, L A, Boon, C
• Format: Journal Article
• Language: English
• Published: Netherlands 1993
• Subjects: Animals; Mutagenesis - physiology; Peptide Elongation Factors - chemistry; Peptide Elongation Factors - physiology; Protein Biosynthesis; Protein Conformation; Ribosomes - physiology; Sequence Homology, Amino Acid; Structure-Activity Relationship
• ISSN: 0300-5208

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.