Research Topics
| M C GanozaSummaryAffiliation: University of Toronto Country: Canada Publications
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Detail Information
Publications
A ribosomal ATPase is a target for hygromycin B inhibition on Escherichia coli ribosomesM C Ganoza
Banting and Best Department of Medical Research, University of Toronto, 112 College St, Toronto, Ontario M5G 1L6, Canada
Antimicrob Agents Chemother 45:2813-9. 2001..The binding site of hygromycin B and its known dual effect on the fidelity of decoding and translocation suggest a model for the action of this drug on ribosomes...
The ribosome as affinity matrix': efficient purification scheme for translation factorsM C Ganoza
Banting and Best Department of Medical Research, University of Toronto, Ontario, Canada
Biochimie 78:51-61. 1996..The procedure markedly simplifies the isolation, in homogeneous form, of all the non-ribosomal proteins required to reconstruct translation...- Identification of a ribosomal ATPase in Escherichia coli cellsM C Kiel
Banting and Best Department of Medical Research, University of Toronto, Ontario, Canad
Biochimie 81:1097-108. 1999..The discovery of a ribosomal ATPase in a prokaryotic cell suggests a common, conserved function for these proteins in translation... - A proposed role for IF-3 and EF-T in maintaining the specificity of prokaryotic initiation complex formationM C Ganoza
Banting and Best Department of Medical Research, University of Toronto, Ontario Canada
Mol Biol Rep 15:33-8. 1991..We propose that one function of EF-T may be to prevent the entry of aminoacyl-tRNAs into the 30S particle during initiation. The possibility that a special site for fMet-tRNA resides on 16S rRNA is also discussed... - Molecular localization of a ribosome-dependent ATPase on Escherichia coli ribosomesJ Xu
Banting and Best Department of Medical Research, University of Toronto, 112 College Street, Toronto, Ontario, Canada M5G 1L6
Nucleic Acids Res 34:1158-65. 2006..The combined data suggest plausible mechanisms for the function of RbbA in translation... - Regulation of gene expression at the translational level. The rescue factor reverses thermosensitive protein synthesis in N4316, a conditionally-lethal mutant of Escherichia coli defective in translationM C Ganoza
Banting and Best Department of Medical Research, C H Best Institute, Toronto, Ontario, Canada
Eur J Biochem 178:663-74. 1989..Based on these and other observations, we propose tht rescue mediates a novel function in the association/dissociation of ribosomal subunits which is essential to the accuracy and efficiency of translation... - Functional interactions of an Escherichia coli ribosomal ATPaseM C Kiel
Banting and Best Department of Medical Research, University of Toronto, 112 College Street, ON, Canada M5G 1L6
Eur J Biochem 268:278-86. 2001..A possible role for RbbA in protein-chain elongation is proposed... - A new factor from Escherichia coli affects translocation of mRNAM C Ganoza
Banting and Best Department of Medical Research, University of Toronto, Ontario, Canada
J Biol Chem 270:26377-81. 1995..We propose that W functions by ejecting tRNAs from ribosomes in a step that precedes the movement of mRNA during translocation... - Molecular characterization of the prokaryotic efp gene product involved in a peptidyltransferase reactionH Aoki
Banting and Best Department of Medical Research, University of Toronto, Ontario, Canada
Biochimie 79:7-11. 1997..This observation and the requirement for L16 but not for the L7/L12 nor L6 or L11 r-proteins suggest that the binding site for EF-P may overlap the peptidyltransferase center of the ribosome... - The gene encoding the elongation factor P protein is essential for viability and is required for protein synthesisH Aoki
Banting and Best Department of Medical Research, Nucleic Acids, Protein Synthesis and Molecular Genetics, University of Toronto, Toronto, Ontario M5G 1L6, Canada
J Biol Chem 272:32254-9. 1997..At 44 degrees C, mutant cells are severely defective in peptide-bond formation. We conclude that the efp gene is essential for cell viability and is required for protein synthesis... - Molecular characterization of a prokaryotic translation factor homologous to the eukaryotic initiation factor eIF4AJ Lu
Banting and Best Department of Medical Research, University of Toronto, Ont, Canada
Int J Biochem Cell Biol 31:215-29. 1999..The W2 protein is not required in standard initiation assays programmed by synthetic mRNAs of defined sequence that lack this feature. We conclude that W2 is an important factor for initiation in eukaryotic and prokaryotic cells... - Peptide bond synthesis: function of the efp gene productM C Ganoza
Banting and Best Department of Medical Research, University of Toronto, Ontario, Canada
Biol Chem 381:553-9. 2000.... - Cloning, sequencing and overexpression of the gene for prokaryotic factor EF-P involved in peptide bond synthesisH Aoki
Banting and Best Department of Medical Research, University of Toronto, Ontario, Canada
Nucleic Acids Res 19:6215-20. 1991..Based on DNA sequence analysis of this gene, the EF-P protein consists of 187 amino acids with a calculated molecular weight of 20,447. The sequence and chromosomal location of EF-P establishes it as a unique gene product... - The asparaginyl-tRNA synthetase gene encodes one of the complementing factors for thermosensitive translation in the Escherichia coli mutant strain, N4316H Aoki
Banting and Best Department of Medical Research, University of Toronto, Ontario, Canada
Eur J Biochem 209:511-21. 1992..A potential role of this synthetase in restoring normal protein synthesis with respect to ribosomal frameshifting, read-through of nonsense codons and protein copy number is discussed... - Characterization and site of action of a soluble protein that stimulates peptide-bond synthesisB R Glick
Eur J Biochem 71:483-91. 1976..Unlike all other propagation factors, EF-P does not require the 50-S ribosomal proteins L7 and L12 and may therefore occupy a different ribosomal site... - Identification and quantitation of elongation factor EF-P in Escherichia coli cell-free extractsG An
Can J Biochem 58:1312-4. 1980..It is also shown that a highly purified preparation of EF-P is free of all known protein synthesis factors and ribosomal proteins... - Isolation of a soluble factor needed for protein synthesis with various messenger ribonucleic acids other than poly(U)M C Ganoza
J Biol Chem 249:1037-43. 1974 - Stimulation of peptidyltransferase reactions by a soluble proteinM C Ganoza
Eur J Biochem 146:287-94. 1985..30S subunits were resistant to treatment by this reagent. These results suggest the involvement of histidine residues in peptidyltransferase activities. The role of EF-P in the catalytic mechanism of peptidyltransferase is discussed... - Identification of a soluble protein that stimulates peptide bond synthesisB R Glick
Proc Natl Acad Sci U S A 72:4257-60. 1975..We suggest that this extraribosomal factor modulates the intrinsic activity of ribosomes to catalyze peptide-bond synthesis, and regard it as a new factor required for peptide chain elongation, which we call EF-P... - Peptide bond formation stimulated by protein synthesis factor EF-P depends on the aminoacyl moiety of the acceptorB R Glick
Eur J Biochem 97:23-8. 1979..One role of EF-P in protein synthesis may be to allow peptide bond synthesis to occur more efficiently with some aminoacyl-tRNAs that are poor acceptors for the ribosomal peptidyl transferase... - Purification and Best Department of Medical Research, University of Toronto, Ont., CanadaB R Glick
Can J Biochem 57:749-57. 1979..1 nm), and a frictional coefficient of 1.48, suggesting an asymmetric structure. By this and a number of other criteria, EF-P is a new factor that controls peptide bond formation during protein biosynthesis...