Results 211 to 220 of about 82,531 (244)
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Fluoroaluminates do not affect the guanine‐nucleotide binding centre of the peptide chain elongation factor EF‐Tu

European Journal of Biochemistry, 1990
EF‐Tu is often referred to as a model for guanine‐nucleotide‐binding regulatory proteins (G‐proteins), since X‐ray diffraction analysis of its GTP‐binding domain shows a detailed location of the ‘consensus’ amino acid sequences involved in nucleotide binding.
B, Kraal   +5 more
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Amino acid sequences of two sulfhydryl-containing tryptic peptides of the polypeptide chain elongation factor Tu

Biochemical and Biophysical Research Communications, 1975
The primary structure around the sulfhydryl groups of the polypeptide chain elongation factor Tu has been investigated. The tryptic peptides containing sulfhydryl groups were separated from other peptides by affinity chromatography using a p-chloromercuribenzoate-agarose column.
S, Nakamura   +3 more
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Functional Role and Biochemical Properties of Yeast Peptide Elongation Factor 3 (EF-3)

1990
The eukaryotic peptide elongation cycle is well known to be driven by the two complementary factors EF-lα and EF-2, functionally analogous to the bacterial EF-Tu and EF-G, respectively, and the two GTP hydrolysis steps catalyzed by those factors have been considered to be essential for the cycle to run (Kaziro, 1978; Moldave, 19 85). On yeast ribosomes,
Masazumi Miyazaki   +4 more
openaire   +1 more source

Soluble factor requirements for the Tetrahymena peptide elongation system and the ribosomal ATPase as a counterpart of yeast elongation factor 3 (EF-3).

Journal of biochemistry, 1991
Peptide elongation factor 3 (EF-3), which is widely present in yeasts and fungi (Eumycota), does not occur in another lower eukaryote, the unicellular protozoan Tetrahymena pyriformis, as was shown by the following findings: (a) there is no activity to satisfy the EF-3 requirement of yeast ribosomes in the post-ribosomal supernatant fraction from ...
M, Miyazaki, H, Kagiyama
openaire   +1 more source

BnEPFL6, an EPIDERMAL PATTERNING FACTOR-LIKE (EPFL) secreted peptide gene, is required for filament elongation in Brassica napus

Plant Molecular Biology, 2014
Inflorescence architecture, pedicel length and stomata patterning in Arabidopsis thaliana are specified by inter-tissue communication mediated by ERECTA and its signaling ligands in the EPIDERMAL PATTERNING FACTOR-LIKE (EPFL) family of secreted cysteine-rich peptides. Here, we identified and characterized BnEPFL6 from Brassica napus.
Yi, Huang   +6 more
openaire   +2 more sources

Purification and enzymatic peptide mapping of protein synthesis elongation factor‐2 from mink and chicken livers

IUBMB Life, 1996
AbstractThis investigation has shown it is possible to purify elongation factor‐2 from livers of two rather distinct animal species, minks and chicken, to high homogeneity by employing the same purification procedure. It is also shown that making peptide maps of the factor by the use of Staphylococcus aureus Endoprotease Glu‐C gives the same pattern ...
openaire   +2 more sources

cDNA sequence of a translational elongation factor Ts homologue from Caenorhabditis elegans: mitochondrial factor-specific features found in the nematode homologue peptide

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1997
The cDNA for a homologue of elongation factor Ts which probably functions in mitochondria has been sequenced from a nematode Caenorhabditis elegans. The deduced amino acid sequence (316 amino acids long) has a possible transit peptide sequence at the amino terminus and several common specific features for mammalian mitochondrial EF-Ts.
Y, Watanabe   +3 more
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[36] Isolation of peptide chain elongation factors from the yeast Saccharomyces cerevisiae (strain kaneka)

1971
Publisher Summary This chapter describes the assay methods for amino acid polymerization, GTP hydrolysis, formation of a GTP-protein complex, and the GTP-dependent binding of phenylalanyl-tRNA to ribosomes; the isolation of the supernatant fluid containing the elongation factors FI and FII from yeast cell; the separation of the elongation factors ...
Dietmar Richter, Friedrich Klink
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Role of yeast peptide elongation factor 3 (EF-3) at the AA-tRNA binding step.

Journal of biochemistry, 1989
The stimulatory effect of peptide elongation factor 3 (EF-3), which is uniquely required for the yeast elongation cycle, on the step of binding of aminoacyl-tRNA (AA-tRNA) to ribosomes has been investigated in detail. Yeast EF-1 alpha apparently functions in a stoichiometric manner in the binding reaction of AA-tRNA to the ribosomes. The addition of EF-
M, Uritani, M, Miyazaki
openaire   +1 more source

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