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PMID: 8109930 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Effect of mutational alteration of Asn-128 in the putative GTP-binding domain of tetracycline resistance determinant Tet(O) from Campylobacter jejuni.

Antimicrobial agents and chemotherapy ·Vol. 37 ·No. 12 ·1993-12-00 ·Pages 2645-9

Grewal J, Manavathu EK, Taylor DE

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.

Related Genes
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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24 references, click to expand
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Article Info
Journal
Antimicrobial agents and chemotherapy
Abbr.
Antimicrob Agents Chemother
ISSN
0066-4804
Published
1993-12-00
Pages
2645-9
Language
English
Region
United States
NLM ID
0315061
PMCID
PMC192766
Subset
IM
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