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Converting GTP hydrolysis into motion: versatile translational elongation factor G.
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- Author(s): Rodnina MV;Rodnina MV; Peske F; Peske F; Peng BZ; Peng BZ; Belardinelli R; Belardinelli R; Wintermeyer W; Wintermeyer W
- Source:
Biological chemistry [Biol Chem] 2019 Dec 18; Vol. 401 (1), pp. 131-142.- Publication Type:
Journal Article; Research Support, Non-U.S. Gov't; Review- Language:
English - Source:
- Additional Information
- Source: Publisher: Walter De Gruyter Country of Publication: Germany NLM ID: 9700112 Publication Model: Print Cited Medium: Internet ISSN: 1437-4315 (Electronic) Linking ISSN: 14316730 NLM ISO Abbreviation: Biol Chem Subsets: MEDLINE
- Publication Information: Publication: Berlin : Walter De Gruyter
Original Publication: Berlin ; New York : W. De Gruyter, c1996- - Subject Terms: Guanosine Triphosphate/*biosynthesis ; Peptide Elongation Factor G/*genetics ; Protein Biosynthesis/*genetics ; Ribosomes/*genetics; GTP Phosphohydrolases/genetics ; Guanosine Triphosphate/genetics ; Hydrolysis ; Peptide Elongation Factor G/biosynthesis ; RNA, Messenger/genetics ; RNA, Transfer/genetics
- Abstract: Elongation factor G (EF-G) is a translational GTPase that acts at several stages of protein synthesis. Its canonical function is to catalyze tRNA movement during translation elongation, but it also acts at the last step of translation to promote ribosome recycling. Moreover, EF-G has additional functions, such as helping the ribosome to maintain the mRNA reading frame or to slide over non-coding stretches of the mRNA. EF-G has an unconventional GTPase cycle that couples the energy of GTP hydrolysis to movement. EF-G facilitates movement in the GDP-Pi form. To convert the energy of hydrolysis to movement, it requires various ligands in the A site, such as a tRNA in translocation, an mRNA secondary structure element in ribosome sliding, or ribosome recycling factor in post-termination complex disassembly. The ligand defines the direction and timing of EF-G-facilitated motion. In this review, we summarize recent advances in understanding the mechanism of EF-G action as a remarkable force-generating GTPase.
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- Accession Number: 0 (Peptide Elongation Factor G)
0 (RNA, Messenger)
86-01-1 (Guanosine Triphosphate)
9014-25-9 (RNA, Transfer)
EC 3.6.1.- (GTP Phosphohydrolases) - Publication Date: Date Created: 20191011 Date Completed: 20200820 Latest Revision: 20210611
- Publication Date: 20221213
- Accession Number: 10.1515/hsz-2019-0313
- Accession Number: 31600135
- Source:
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