Topic
EF-Ts
About: EF-Ts is a research topic. Over the lifetime, 38 publications have been published within this topic receiving 1990 citations. The topic is also known as: EF-Ts_dimer_sf & IPR036402.
Papers
TL;DR: Subunit III is shown to be identical to the protein synthesis elongation factor EF Tu by the following criteria: coelectrophoresis on sodium dodecyl sulfate gels, precipitation ofEF Tu by anti-Qbeta replicase serum, binding of guanine nucleotides, and binding of phenylalanyl-tRNA.
Abstract: The enzyme, Qbeta replicase, responsible for the replication of the RNA of Escherichia coli pahge Qbeta, is composed of four nonidentical subunits, three of which, I, III, and IV, are coded for by the bacterial genome, while subunit II is phage-specific. SUBUNIT IV IS SHOWN TO BE IDENTICAL TO THE PROTEIN SYNTHESIS ELONGATION FACTOR EF TS BY THE FOLLOWING CRITERIA: coelectrophoresis on polyacrylamide gels in sodium dodecyl sulfate and in urea buffers, identity of the first seven amino acids at the amino-terminus, precipitation of sub-unit IV by anti-EF T-factor serum, and stimulation of EF Tu-GDP exchange by subunit IV. Subunit III is shown to be identical to the protein synthesis elongation factor EF Tu by the following criteria: coelectrophoresis on sodium dodecyl sulfate gels, precipitation of EF Tu by anti-Qbeta replicase serum, binding of guanine nucleotides, and binding of phenylalanyl-tRNA. In addition, Qbeta replicase activity can be reconstituted from subunits I and II with EF Tu and EF Ts.
249 citations
TL;DR: The crystal structure of the complex formed by the elongation factor Tu ( EF-Tu) and its exchange factor Ts (EF-Ts) from Thermus thermophilus is determined and may have useful implications for receptor-induced exchange in heterotrimeric G proteins.
Abstract: In order to study nucleotide exchange mechanisms in GTP-binding proteins, we have determined the crystal structure of the complex formed by the elongation factor Tu (EF-Tu) and its exchange factor Ts (EF-Ts) from Thermus thermophilus The complex is a dyad symmetrical heterotetramer in which each EF-Tu, through a bipartite interface, interacts with two subunits of EF-Ts, explaining the need for a dimeric exchange factor The architecture of the assembly is distinctly different from that of the corresponding heterodimeric E coli complex, in which the monomeric E coli EF-Ts remarkably forms essentially the same bipartite interface with EF-Tu through a sequence/structural repeat GDP is released primarily by a Ts-induced peptide flip in the nucleotide binding pocket that disrupts hydrogen bonds to the phosphates and repositions the peptide carbonyl so as to sterically and electrostatically eject the GDP The exchange mechanism may have useful implications for receptor-induced exchange in heterotrimeric G proteins
125 citations
TL;DR: The C-terminal extension of mitochondrial EF-Tu has structural similarities with DNA recognising zinc fingers suggesting that the extension may be involved in recognition of RNA.
65 citations
TL;DR: In this article, the rate constants of the multistep reaction between Escherichia coli EF-Tu, EF-Ts, and GDP were determined by stopping-flow kinetic analysis monitoring the fluorescence of either Trp-184 in EF- Tu or mant-GDP.
64 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2021 | 1 |
| 2013 | 2 |
| 2011 | 1 |
| 2010 | 1 |
| 2007 | 1 |
| 2002 | 3 |