Results 201 to 210 of about 82,531 (244)
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Specificity of elongation factor EF-TU for hydrophobic peptides
Biochemical and Biophysical Research Communications, 2002The 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 +4 more
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CTP can replace GTP in reactions catalyzed by eukaryotic peptide elongation factor 1 [PDF]
FEBS Letters, 1984 In several reactions catalyzed by highly purified peptide elongation factor 1 from rabbit reticulocytes, GTP may be fully replaced by CTP but not by ATP or UTP. This holds true for the factor‐dependent binding of aminoacyl‐tRNA to ribosomes, GTPase activity, GTP‐dependent autophosphorylation of the factor protein and binding of cholesteryl 14 ...
Tuháčková, Z. +2 more
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A mutant of Escherichia coli blocked in peptide elongation: Altered elongation factor Ts
Journal of Molecular Biology, 1974Abstract 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
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Journal of Biochemistry, 1989
The cytoplasmic peptide elongation factor, EF-1 alpha, is anchored at the endoplasmic reticulum membrane by phosphatidylinositol via ethanolamine bridging presumably to Asp306 of the protein.
Shigeru Utsumi +2 more
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The cytoplasmic peptide elongation factor, EF-1 alpha, is anchored at the endoplasmic reticulum membrane by phosphatidylinositol via ethanolamine bridging presumably to Asp306 of the protein.
Shigeru Utsumi +2 more
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The Journal of Biochemistry, 1988
Cytoplasmic elongation factor 1 alpha (EF-1 alpha) [corrected] was purified to homogeneity in high yield from the two different yeasts Saccharomyces carlsbergensis (S. carls.) and Schizosaccharomyces pombe (S. pombe). The purification was easily achieved by CM-Sephadex column chromatography of the breakthrough fractions from DEAE-Sephadex ...
M, Miyazaki +5 more
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Cytoplasmic elongation factor 1 alpha (EF-1 alpha) [corrected] was purified to homogeneity in high yield from the two different yeasts Saccharomyces carlsbergensis (S. carls.) and Schizosaccharomyces pombe (S. pombe). The purification was easily achieved by CM-Sephadex column chromatography of the breakthrough fractions from DEAE-Sephadex ...
M, Miyazaki +5 more
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A novel reaction of reticulocyte peptide-chain elongation factor, EF2, with guanosine nucleotides
Archives of Biochemistry and Biophysics, 1973Abstract 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
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European Journal of Biochemistry, 1985
The binding of [3H]cholesteryl 14‐methylhexadecanoate by a highly purified peptide elongation factor 1 from rabbit reticulocytes is significantly enhanced by GTP and CTP, much less by guanosine 5′‐[β,γ‐methylene]‐triphosphate and not at all by ATP or UTP.
Z, Tuhácková, J, Hradec
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The binding of [3H]cholesteryl 14‐methylhexadecanoate by a highly purified peptide elongation factor 1 from rabbit reticulocytes is significantly enhanced by GTP and CTP, much less by guanosine 5′‐[β,γ‐methylene]‐triphosphate and not at all by ATP or UTP.
Z, Tuhácková, J, Hradec
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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 +3 more
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At least two molecules of GTP may be hydrolysed during the addition of an amino-acid to a growing peptide chain.
Y, Ono +3 more
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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 +3 more
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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 +3 more
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Journal of Molecular Biology, 2008
The elongation stage of protein synthesis consists of repeated cycles of the binding of aminoacyl-tRNA, peptide bond formation, and translocation. The process is normally catalyzed by the elongation factors Tu and G; however, the reactions can proceed, at least in prescribed and limited circumstance, in the absence of the elongation factors, a finding ...
Yuen-Ling Chan, Ira G Wool
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The elongation stage of protein synthesis consists of repeated cycles of the binding of aminoacyl-tRNA, peptide bond formation, and translocation. The process is normally catalyzed by the elongation factors Tu and G; however, the reactions can proceed, at least in prescribed and limited circumstance, in the absence of the elongation factors, a finding ...
Yuen-Ling Chan, Ira G Wool
exaly +3 more sources