title: Effect of mutational alteration of Asn-128 in the putative GTP-binding domain of tetracycline resistance determinant Tet(O) from Campylobacter jejuni.
abstract: The deduced amino acid sequence of Campylobacter jejuni Tet(O), cloned in Escherichia coli, has shown that it contains the five highly conserved sequences of the GTP-binding domain found in other GTPases. Asn-128 belongs to the G4 motif of such a domain and is involved in hydrogen bonding with the guanine ring of the nucleotide. Substitution of Asn-128 by 11 other amino acids resulted in a decrease in tetracycline resistance, indicating that tetracycline resistance conferred by Tet(O) is related to GTP binding. The effect of the mutations on the GTP-binding domain is discussed with the EF-Tu-GDP complex as a model.
authors.affiliation: Department of Medical Microbiology and Infectious Diseases, University of Alberta, Edmonton, Canada.
authors.forename: J
authors.initials: J
authors.lastname: Grewal
authors.forename: E K
authors.initials: EK
authors.lastname: Manavathu
authors.forename: D E
authors.initials: DE
authors.lastname: Taylor
mesh_terms: D000595:Amino Acid Sequence; D001216:Asparagine / Q000235:genetics*; D001665:Binding Sites; D016123:Campylobacter jejuni / Q000187:drug effects / Q000235:genetics* / Q000502:physiology; D019204:GTP-Binding Proteins / Q000235:genetics*; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009154:Mutation / Q000235:genetics*; D010452:Peptide Biosynthesis; D010455:Peptides; D011072:Poly U / Q000494:pharmacology; D012270:Ribosomes / Q000378:metabolism; D013753:Tetracycline Resistance / Q000235:genetics*; D013754:Tetracyclines / Q000378:metabolism / Q000494:pharmacology
chemical_list: D010455:Peptides; D013754:Tetracyclines; D011072:Poly U; C012001:polyphenylalanine; D001216:Asparagine; D019204:GTP-Binding Proteins