Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 65, Issue 9, Pages 1335-1346Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-008-7495-6
Keywords
elongation factor; release factor; termination factor; ribosome structure; GTPase; protein synthesis
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The elongation and termination steps of protein synthesis are controlled by elongation and release factors, respectively. Elongation factors deliver the aminoacyl tRNA to the ribosomal A site, ensuring the elongation of the nascent polypeptide chain by one amino acid at a time, while release factors recognize the stop codons and trigger the release of the polypeptide from the ribosome. Recently, high-resolution crystal structures of ribosomes as well as translation factors on and off the ribosome have contributed a great deal to our understanding of the molecular basis of protein synthesis. This review concentrates on recent developments in our understanding of the elongation and termination steps of protein synthesis, particularly the roles of translation factors and their similarities and differences in the eukaryotic cytosol and prokaryotic systems, through a combination of structural and biochemical studies.
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