Results 161 to 170 of about 359,289 (223)

Peptide Chain Elongation: GTP Cleavage catalysed by Factors binding Aminoacyl-Transfer RNA to the Ribosome

Nature, 1969
At least two molecules of GTP may be hydrolysed during the addition of an amino-acid to a growing peptide chain.
Y. Ono, A. Skoultchi, J. Waterson, P. Lengyel   +3 more
semanticscholar   +3 more sources

Peptide Chain Elongation: Discrimination against the Initiator Transfer RNA by Microbial Amino-acid Polymerization Factors

Nature, 1968
The amino-acid polymerization factors S1 and S3 form complexes with most aminoacyl-tRNA species, including met-tRNAM, but not F-met-tRNAF and not met-tRNAF. This discrimination may be a basis for avoiding one kind of ambiguity in translation.
Y. Ono, A. Skoultchi, Albrecht Klein, P. Lengyel   +3 more
semanticscholar   +3 more sources

Separation of mitochondrial and cytoplasmic peptide chain elongation factors from yeast.

Biochemistry, 1970
D. Richter, F. Lipmann
semanticscholar   +3 more sources

Production of mitochondrial peptide-chain elongation factors in yeast deficient in mitochondrial deoxyribonucleic acid.

Biochemistry, 1971
D. Richter
semanticscholar   +3 more sources

The S1 Factor in Peptide Chain Elongation

Nature, 1970
Aminoacyl-tRNA becomes attached to the ribosome as part of an S3 factor–GTP–aminoacyl-tRNA complex. GTP is then cleaved and an S3 factor–GDP complex is released. The S1 factor promotes the re-formation of the S3 factor–GTP–aminoacyl-tRNA complex from the S3 factor–GDP complex, aminoacyl-tRNA and GTP.
J, Waterson, G, Beaud, P, Lengyel
openaire   +2 more sources

Specificity of elongation factor EF-TU for hydrophobic peptides

Biochemical and Biophysical Research Communications, 2002
The elongation factor EF-Tu carries aminoacyl-tRNAs to the A-site of the ribosome during the elongation process of protein biosynthesis. We, and others, have recently reported that the Escherichia coli EF-Tu interacts with unfolded and denatured proteins and behaves like a chaperone in protein folding and protection against protein thermal denaturation.
Abdelharim, Malki, Teresa, Caldas, Andrea, Parmeggiani, Masamichi, Kohiyama, Gilbert, Richarme   +4 more
openaire   +2 more sources

Role of elongation factor 2 in regulating peptide-chain elongation in the heart

American Journal of Physiology-Endocrinology and Metabolism, 1994
Cardiac muscles of experimentally induced diabetic rats show a progressive decrease in the rate of protein synthesis. The decline in protein synthesis is associated with decreases in both the number and efficiency of cardiac ribosomes. In hearts from 48 h diabetic rats, the decrease in protein synthesis was accounted for solely by a 28% reduction in ...
T C, Vary, A, Nairn, C J, Lynch
openaire   +2 more sources

A mutant of Escherichia coli blocked in peptide elongation: Altered elongation factor Ts

Journal of Molecular Biology, 1974
Abstract Among our transfer RNA-dependent growth mutants, one, HAK88, was found that carries an altered elongation factor Ts. The activity of mutant EFTs to bind GDP to EFTu, or to form the ternary complex (aminoacyl-tRNA-EFTu-GTP) is thermolabile. The effect of magnesium on the formation of EFTu-GDP from the EFTu-EFTs complex of HAK8 shows that a ...
M, Kuwano, H, Endo, T, Kamiya, K, Hori
openaire   +2 more sources

A New Concept of the Function of Elongation Factor 1 in Peptide Chain Elongation

European Journal of Biochemistry, 1976
An entirely new model for the mechanism of elongation factor 1 (EF‐1) function is presented. Experiments, in which mixtures of [3H]EF‐1, ribosomes from Krebs II ascites cells and various additional co‐factors were analyzed by chromatography on Sepharose 6B, show that EF‐1 binds to the ribosome early in the translation process and remains bound on the ...
H, Grasmuk, R D, Nolan, J, Drews
openaire   +2 more sources

A novel reaction of reticulocyte peptide-chain elongation factor, EF2, with guanosine nucleotides

Archives of Biochemistry and Biophysics, 1973
Abstract The formation of phenylalanyl puromycin from phenylalanyl-tRNA, bound nonenzymically or enzymically to reticulocyte ribosomes, requires the peptide-chain elongation factor, EF2 2 , and GTP. However the GTP analogue, GDPCP, may replace GTP to a significant extent in this reaction.
T, Lee, P, Tsai, R, Heintz
openaire   +2 more sources