Identification of a histidine residue near the aminoacyl transfer ribonucleic acid binding site of elongation factor Tu.

No abstract is available for this paper.

• Publication year

  1981

• Venue

  Biochemistry

• Publication date

  1981-08-04

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1021/BI00519A022PMID 6913406
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Separation of opioid peptides utilizing high performance liquid chromatography.

  2009cited by this paper
• Elongation factor-dependent affinity labeling of Escherichia coli ribosomes.

  1980cited by this paper
• Chemical evidence for the involvement of histidyl residues in the functioning of Escherichia coli elongation factor Tu

  1980cited by this paper
• Proton nuclear magnetic resonance study on the roles of histidine residues in the binding of polypeptide chain elongation factor Tu from Thermus thermophilus with aminoacyl transfer ribonucleic acid and guanine nucleotides.

  1980cited by this paper
• Biochemical and structural studies of the tetragonal crystalline modification of the Escherichia coli elongation factor Tu.

  1980cited by this paper
• Composition and properties of trypsin-cleaved elongation factor Tu.

  1980cited by this paper
• The complete amino-acid sequence of elongation factor Tu from Escherichia coli.

  1980cited by this paper
• Primary structure of elongation factor Tu from Escherichia coli.

  1980cited by this paper
• Functional covalent complex between elongation factor Tu and an analog of lysyl-tRNA.

  1978cited by this paper
• High resolution x-ray crystallographic analysis of a modified form of the elongation factor Tu: guanosine diphosphate complex.

  1978cited by this paper
• The evolution of elongation factors Tu and G by gene duplication

  1978cited by this paper
• Amino acid sequence of elongation factor Tu. Characterization and alignment of the cyanogen bromide fragments and location of the cysteine residues

  1977cited by this paper
• [34] Improved manual sequencing methods

  1977cited by this paper
• Crystals of a large tryptic peptide (fragment A) of elongation factor EF‐Tu from Escherichia coli

  1977cited by this paper
• Improved manual sequencing methods.

  1977cited by this paper
• Limited hydrolysis of the polypeptide chain elongation factor Tu by trypsin. Isolation and characterization of the polypeptide fragments.

  1976cited by this paper
• Nomenclature of α-amino acids. (Recommendations, 1974)

  1975cited by this paper
• Amino acid sequence of elongation factor Tu. Sequence of a region containing the thiol group essential for GTP binding

  1975cited by this paper
• Automatic Monitoring of primary amines in preparative column effluents with fluorescamine.

  1975cited by this paper
• Elongation factor Tu and the aminoacyl-tRNA-EFTu-GTP complex.

  1974cited by this paper
• Amino acid analysis with fluorescamine at the picomole level.

  1973cited by this paper
• The reactions of the sulfhydryl groups on the elongation factors Tu and Ts.

  1971cited by this paper
• Alkylation and identification of the histidine residues at the active site of ribonuclease.

  1963cited by this paper
• The nature of the amino acid residues involved in the inactivation of ribonuclease by iodoacetate.

  1959cited by this paper

• Translation Elongation Factor 1A Mutants with Altered Actin Bundling Activity Show Reduced Aminoacyl-tRNA Binding and Alter Initiation via eIF2α Phosphorylation*

  2014cites this paper
• The effect of mutations in EF-Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability.

  2000cites this paper
• Possible evolution of factors involved in protein biosynthesis.

  1998cites this paper
• The ternary complex of EF-Tu and its role in protein biosynthesis.

  1997cites this paper
• Macromolecular mimicry in protein biosynthesis.

  1997cites this paper
• The ternary complex of aminoacylated tRNA and EF-Tu-GTP. Recognition of a bond and a fold.

  1996cites this paper
• Mapping Escherichia coli Elongation Factor Tu Residues Involved in Binding of Aminoacyl-tRNA*

  1996cites this paper
• Elongation in bacterial protein biosynthesis.

  1996cites this paper
• A complex profile of protein elongation: translating chemical energy into molecular movement.

  1996cites this paper
• Structure of the ternary complex of EF-Tu: macromolecular mimicry in translation.

  1996cites this paper
• Macromolecular arrangement in the aminoacyl-tRNA.elongation factor Tu.GTP ternary complex. A fluorescence energy transfer study.

  1995cites this paper
• Mutations in GCD11, the structural gene for eIF‐2 gamma in yeast, alter translational regulation of GCN4 and the selection of the start site for protein synthesis.

  1995cites this paper
• Recognition of Aminoacyl-tRNAs by Protein Elongation Factors

  1995cites this paper
• Properties of isolated domains of the elongation factor Tu from Thermus thermophilus HB8.

  1995cites this paper
• Minimalist aminoacylated RNAs as efficient substrates for elongation factor Tu.

  1994cites this paper
• Towards an understanding of structure‐function relationships of elongation factor Tu

  1994cites this paper
• Histidine‐118 of elongation factor Tu: its role in aminoacyl‐tRNA binding and regulation of the GTPase activity

  1994cites this paper
• Three tuf-like genes in the kirromycin producer Streptomyces ramocissimus.

  1994cites this paper
• Escherichia coli elongation-factor-Tu mutants with decreased affinity for aminoacyl-tRNA.

  1994cites this paper
• Topography of the Ternary EF-Tu/GTP/Phe-tRNAPhe Complex as Studied by Crosslinking and Limited Proteolysis

  1993cites this paper
• Crystal structure of active elongation factor Tu reveals major domain rearrangements

  1993cites this paper
• Ternary complex between elongation factor Tu.GTP and Phe-tRNA(Phe).

  1993cites this paper
• Altered lead(II)-cleavage pattern of free Phe-tRNAPhe and Phe-tRNAPhe in ternary complex with EF-Tu:GTP.

  1993cites this paper
• Protein Synthesis and Secretion as Seen by the Nascent Protein Chain

  1993cites this paper
• A single amino acid substitution in elongation factor Tu disrupts interaction between the ternary complex and the ribosome

  1993cites this paper
• Site-directed mutagenesis of elongation factor Tu. The functional and structural role of residue Cys81.

  1992cites this paper
• Isolation and functional analysis of histidine-tagged elongation factor Tu.

  1992cites this paper
• A model for the aminoacyl-tRNA binding site of eukaryotic elongation factor 1 alpha.

  1992cites this paper
• Missense substitutions lethal to essential functions of EF-Tu.

  1991cites this paper
• Interaction of the isolated domain II/III of Thermus thermophilus elongation factor Tu with the nucleotide exchange factor EF-Ts.

  1990cites this paper
• Mapping the effector region in Thermus thermophilus elongation factor Tu.

  1990cites this paper
• Translational dynamics. Interactions between the translational factors, tRNA and ribosomes during eukaryotic protein synthesis.

  1990cites this paper
• Genetic engineering, isolation and characterization of a truncated Escherichia coli elongation factor Tu comprising domains 2 and 3.

  1990cites this paper
• The influence of different modifications of elongation factor Tu from Escherichia coli on ternary complex formation investigated by fluorescence spectroscopy.

  1990cites this paper
• Review Translational dynamics

  1990cites this paper
• Protein translocation across the endoplasmic reticulum membrane: identification by photocross-linking of a 39-kD integral membrane glycoprotein as part of a putative translocation tunnel

  1989cites this paper
• Crosslinking of elongation factor Tu to tRNAPhe by trans‐diamminedichloroplatinum (II) Characterization of two crosslinking sites on EF‐Tu

  1989cites this paper
• Time-resolved fluorescence studies on the ternary complex formed between bacterial elongation factor Tu, guanosine 5'-triphosphate, and phenylalanyl-tRNAPhe.

  1989cites this paper
• Structure-function relationships of elongation factor Tu. Isolation and activity of the guanine-nucleotide-binding domain.

  1989cites this paper
• Fluorescence Investigations on the Elongation Factor Tu System

  1989cites this paper
• Characterization of Elongation Factor Tu from Bacillus Subtilis Modified by Affinity Labelling

  1989cites this paper
• Progress on the Three-Dimensional Structural Determination of Trypsin-Modified EF-TU-GDP

  1989cites this paper
• Covalent coupling of the variable loop of the elongator methionine tRNA to a specific lysine residue in Escherichia coli methionyl-tRNA synthetase.

  1987cites this paper
• A conserved amino acid sequence around Arg-68 of Artemia elongation factor 1 alpha is involved in the binding of guanine nucleotides and aminoacyl transfer RNAs.

  1987cites this paper
• The Aminoacyl-tRNA-Elongation Factor Tu-GTP Ternary Complex and Its Role in Aminoacyl-tRNA Selection at the Ribosome

  1986cites this paper
• A neutron scattering study of the ternary complex EF-Tu.GTP-valyl-tRNAVal1A.

  1986cites this paper
• Photochemical cross-linking of tRNA1Arg to the 30S ribosomal subunit using aryl azide reagents attached to the anticodon loop.

  1985cites this paper
• Effect of trypsin modification of the Escherichia coli elongation factor Tu on the ternary complex with aminoacyl-tRNA.

  1985cites this paper
• Mutant species of EF‐Tu, altered at position 375, exhibit a reduced affinity for aminoacylated transfer‐RNAs

  1985cites this paper
• Amino Acid Residues in Elongation Factor Tu from Escherichia Coli near the Binding Site for the 3′ Terminus of Aminoacyl-tRNA

  1985cites this paper
• Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP.

  1984cites this paper
• Modification of amino groups in EF-Tu.GTP and the ternary complex EF-Tu.GTP.valyl-tRNAVal.

  1984cites this paper
• Histidine residues in elongation factor EF-tu from Escherichia coli protected by aminoacyl-tRNA against photo-oxidation.

  1984cites this paper
• Cross-linking of tRNA at two different sites of the elongation factor Tu.

  1984cites this paper
• Crystallographic Studies of the Protein Biosynthesis System

  1983cites this paper
• Formation and properties of a covalent complex between elongation factor Tu and Phe-tRNA bearing a photoaffinity probe on its 3-(3-amino-3-carboxypropyl)uridine residue.

  1983cites this paper
• The Allosteric Behaviour of the Elongation Factor EF-Tu

  1983cites this paper
• Structural studies of ribosomes.

  1982cites this paper