Effect of mutational alteration of Asn-128 in the putative GTP-binding domain of tetracycline resistance determinant Tet(O) from Campylobacter jejuni.
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.
Grewal
J
J
Department of Medical Microbiology and Infectious Diseases, University of Alberta, Edmonton, Canada.
Manavathu
E K
EK
Taylor
D E
DE
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
D010455:Peptides; D013754:Tetracyclines; D011072:Poly U; C012001:polyphenylalanine; D001216:Asparagine; D019204:GTP-Binding Proteins