Abstract
Elongation factor Tu plays a pivotal role in the elongation cycle of both prokaryotic and eukaryotic protein biosynthesis. The prokaryotic factor in the form of EF-Tu. GTP forms a complex with aminoacyl-tRNA and promotes its binding to the A-site of mRNA-programmed ribosomes. During the reaction, GTP in the complex is hydrolyzed to GDP, and a stable form of EF-Tu, EF-Tu. GDP, which has a low affinity for aminoacyl-tRNA, is released from the ribosome. The recognition of aminoacyl-tRNA, is released from the ribosome. The recognition of aminoacyl-tRNA by EF-Tu represents a natural model for the study of complex interaction processes between nucleic acids and proteins.
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© 1988 Plenum Press, New York
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Jonák, J., Karas, K., Rychlík, I. (1988). Specific Labelling in the Functional Domain of Elongation Factor EF-Tu from Bacillus Stearothermophilus and from Bacillus Subtilis . In: Zelinka, J., Balan, J. (eds) Metabolism and Enzymology of Nucleic Acids. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0749-5_13
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DOI: https://doi.org/10.1007/978-1-4613-0749-5_13
Publisher Name: Springer, Boston, MA
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