Phosphorylation of elongation factor 1 (EF-1) and valyl-tRNA synthetase by protein kinase C and stimulation of EF-1 activity

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Interaction of eukaryote elongation factor EF 1 with guanosine nucleotides and aminoacyl-tRNA.

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Inhibition by elongation factor EF G of aminoacyl-tRNA binding to ribosomes.

Elongation factor G (EF G), bound to ribosomes either with GMPPCP or with fusidic acid and GDP, inhibits elongation factor Tu (EF Tu)-dependent binding of Phe-tRNA on the ribosome-poly(U) complex and binding of Ala-tRNA on the initiation complex formed with RNA from bacteriophage R17; GTP hydrolysis associated with Phe-tRNA binding is also inhibited. Moreover, nonenzymic binding of Phe-tRNA at ...

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Phosphorylation of Human CTP Synthetase 1 by Protein Kinase C IDENTIFICATION OF Ser AND Thr AS MAJOR SITES OF PHOSPHORYLATION*

Phosphorylation of human CTP synthetase 1 by mammalian protein kinase C was examined. Using purified Escherichia coliexpressed CTP synthetase 1 as a substrate, protein kinase C activity was timeand dose-dependent and dependent on the concentrations of ATP and CTP synthetase 1. The protein kinase C phosphorylation of the recombinant enzyme was accompanied by a 95-fold increase in CTP synthetase ...

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Frequency metrology on the EF 1

←X 1 g + 0,0 two-photon transition near 202 nm. For this purpose, the fourth harmonic of an injection-seeded titanium:sapphire pulsed oscillator is employed in a Doppler-free REMPI-detection scheme on a molecular beam of hydrogen. A frequency comb laser is used to perform the absolute frequency calibration on the continuous-wave CW laser that injection-seeds the oscillator. Chirp-induced freque...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1991

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)98937-4