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.
MeSH Terms
Amino Acid Sequence
Asparagine/genetics
Binding Sites
Campylobacter jejuni/drug effects,genetics,physiology
GTP-Binding Proteins/genetics
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation/genetics
Peptide Biosynthesis
Peptides
Poly U/pharmacology
Ribosomes/metabolism
Tetracycline Resistance/genetics
Tetracyclines/metabolism,pharmacology
Chemicals
Peptides
Tetracyclines
Poly U
polyphenylalanine
Asparagine
GTP-Binding Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Grewal J
Department of Medical Microbiology and Infectious Diseases, University of Alberta, Edmonton, Canada.
Manavathu E K
Taylor D E
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