Polymerization of the bacterial elongation factor for protein synthesis, EF-Tu.
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Summary
Electron microscopic observations of negatively stained images demonstrates that the EF-Tu fibrils consist of bundles of individual filaments, approximately 5nm in diameter, aligned parallel to the long axis of the fibril.
- Type
- article
- Published
- 1979-07-01
- Cited by
- 51
- References
- 52
- Access
- Open access
- OpenAlex
- https://openalex.org/W1987498536
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:7327357
Keywords
Elongation, Fibril, Polymerization, Elongation factor, EF-Tu
References
- Conformational transitions of polypeptide chain elongation factor Tu. I. Studies with hydrophobic probes.
- Elongation factor Tu and the aminoacyl-tRNA-EFTu-GTP complex.
- Membrane structures in stable L-forms of Escherichia coli
- Limited proteolysis of elongation factor Tu from Escherichia coli, Multiple intermediates.
- Microtubular structures in a stable staphylococcal L-form
- Formation and properties of the aminoacyl transfer ribonucleic acid-guanosine triphosphate-protein complex.
- Hydrolysis of guanosine 5'-triphosphate associated wh binding of aminoacyl transfer ribonucleic acid to ribosomes.
- Cytoplasmic structure and contractility in amoeboid cells.
- Function and structure in ribonucleic acid phage Qbeta ribonucleic acid replicase. Effect of inhibitors of EF-Tu on ribonucleic acid synthesis and renaturation of active enzyme.
- Paracrystalline arrays of protein-synthesis elongation factor Tu. Comparison with polymerized actin.
- Actin-like properties from Escherichia coli: concept of cytotonus as the missing link between cell metabolism and the biological ion-exchange resin
- Effect of aminoacyl transfer ribonucleic acid on competition between guanosine 5'-triphosphate and guanosine 5'-diphosphate for binding to a polypeptide chain elongation factor from Escherichia coli.
- Precipitation of proteins by vinblastine and calcium ions.
- Properties of a major protein released from Escherichia coli by osmotic shock.
- Peptide Chain Elongation: GTP Cleavage catalysed by Factors binding Aminoacyl-Transfer RNA to the Ribosome
- ELECTRON MICROSCOPE STUDIES ON THE STRUCTURE OF NATURAL AND SYNTHETIC PROTEIN FILAMENTS FROM STRIATED MUSCLE.
- Extraction of an actin-like protein from the prokaryote Mycoplasma pneumoniae.
- Affinity purification of elongation factors tu and Ts
- Two chromatographically separable forms of Escherichia coli elongation factor Tu.
- Determination of protein: a modification of the Lowry method that gives a linear photometric response.
Cited by
- Molecular interactions of Salmonella with the host epithelium in the presence of commensals
- The elongation phase of protein synthesis.
- The development of methods to investigate the mechanisms underlying serum resistance of Ureaplasma species
- Protein synthesis elongation factors Tu and Tu.Ts from Caulobacter crescentus: sensitivity to kirromycin and activity in Q beta replicase
- Refined structure of elongation factor EF-Tu from Escherichia coli.
- Studies on the elongation factor Tu from Streptomyces aureofaciens producing tetracycline.
- Molecular properties of two mutant species of the elongation factor Tu.
- Dynamics and morphology of the in vitro polymeric form of elongation factor Tu from Escherichia coli.
- Bacterial translation elongation factor EF-Tu interacts and colocalizes with actin-like MreB protein
- The complete amino-acid sequence of elongation factor Tu from Escherichia coli.
- A kirromycin resistant elongation factor EF‐Tu from Escherichia coli contains a threonine instead of an alanine residue in position 375
- Effects of a Skin Neuropeptide (Substance P) on Cutaneous Microflora
- Isolation, crystallization and X‐ray analysis of the quaternary complex of Phe‐tRNAPhe, EF‐Tu, a GTP analog and kirromycin
- Molecular properties of elongation factor Tu fromStreptomyces aureofaciens andEscherichia coli
- Structure of the cytoskeleton of Spiroplasma melliferum BC3 and its interactions with the cell membrane.
- INTERACTION OF PLANT POLYSOMES WITH THE ACTIN CYTOSKELETON
- Characterization of regular polymerization products of elongation factor EF-Tu from Escherichia coli by electron microscopy and image processing.
- Isolation and characterization of Streptomyces aureofaciens protein-synthesis elongation factor Tu in an aggregated state.
- Immunocytochemical localization of the elongation factor Tu in E. coli cells
- Polypeptide elongation factor Tu: observations on the interaction with DNase I and the aggregation at pH 6
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