efp Antibody

1. The activity of EF-P is controlled by recognition elements in the tRNA D-arm. PMID: 27216360
2. study of the spatial distribution and ribosome-binding dynamics of EF-P in live E. coli cells; EF-P binds to and unbinds from translating ribosomes during at least 25% of all elongation events; it may bind during every elongation cycle PMID: 28588135
3. Binding of EF-P stabilizes the P-site tRNA, particularly via interactions between its modification and the CCA end, thereby enforcing an alternative conformation of the polyproline-containing nascent chain, which allows a favorable substrate geometry for peptide bond formation. PMID: 29100052
4. In the absence of EF-P, the presence of Rho utilization (rut) sites led to an ~30-fold decrease in translation of polyproline-encoding mRNAs. PMID: 27624127
5. These findings indicate that the ability of a given PPX motif to initiate an EF-P-alleviated stall is strongly influenced by its local context. PMID: 25144653
6. Authors demonstrate that EF-P is dispensable in Escherichia coli and Pseudomonas aeruginosa under laboratory growth conditions. PMID: 23591475
7. Distinct XPPX sequence motifs induce ribosome stalling, which is rescued by the translation elongation factor EF-P. PMID: 24003132
8. EF-P is an elongation factor that enhances translation of polyproline-containing proteins: In the absence of EF-P, ribosomes stall at polyproline stretches, whereas the presence of EF-P alleviates the translational stalling. PMID: 23239623
9. EF-P and its eukaryotic homolog, eIF5A, are essential for the synthesis of a subset of proteins containing proline stretches in all cells. PMID: 23239624
10. GenX-elongation factor P-lysyl adenylate analogue crystals belonged to the monoclinic space group P2(1), with unit-cell parameters a=105.93, b=102.96, c=119.94 A, beta=99.4 degrees, and diffracted to 2.5 A resolution PMID: 20823541
11. reveal that the translation elongation factor P (EF-P) lysylation by GenX is enhanced by YjeK (lysine 2,3-aminomutase paralog) PMID: 20729861

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KEGG: ecj:JW4107

STRING: 316385.ECDH10B_4340