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| Content Provider | Springer Nature Link |
|---|---|
| Author | ble, C. G. Song, H. |
| Copyright Year | 2008 |
| Abstract | 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, highresolution 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. |
| Starting Page | 1335 |
| Ending Page | 1346 |
| Page Count | 12 |
| File Format | |
| ISSN | 1420682X |
| Journal | Cellular and Molecular Life Sciences |
| Volume Number | 65 |
| Issue Number | 9 |
| e-ISSN | 14209071 |
| Language | English |
| Publisher | SP Birkhäuser Verlag Basel |
| Publisher Date | 2008-01-24 |
| Publisher Place | Basel |
| Access Restriction | Subscribed |
| Subject Keyword | Elongation factor release factor termination factor ribosome structure GTPase protein synthesis Biochemistry Life Sciences Biomedicine general Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Molecular Biology Molecular Medicine Pharmacology Cellular and Molecular Neuroscience |
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