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

J. Grewal, E. K. Manavathu, D. E. Taylor

Research output: Contribution to journalArticle

14 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)2645-2649
Number of pages5
JournalAntimicrobial Agents and Chemotherapy
Volume37
Issue number12
DOIs
StatePublished - Jan 1 1993

Fingerprint

Tetracycline Resistance
Campylobacter jejuni
Guanosine Triphosphate
Peptide Elongation Factor Tu
Guanine Nucleotides
Conserved Sequence
GTP Phosphohydrolases
Hydrogen Bonding
Amino Acid Sequence
Escherichia coli
Amino Acids
Mutation

ASJC Scopus subject areas

  • Pharmacology
  • Pharmacology (medical)
  • Infectious Diseases

Cite this

Effect of mutational alteration of Asn-128 in the putative GTP-binding domain of tetracycline resistance determinant Tet(O) from Campylobacter jejuni. / Grewal, J.; Manavathu, E. K.; Taylor, D. E.

In: Antimicrobial Agents and Chemotherapy, Vol. 37, No. 12, 01.01.1993, p. 2645-2649.

Research output: Contribution to journalArticle

@article{307c81fb19b542d6978abeddd02552d2,
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.",
author = "J. Grewal and Manavathu, {E. K.} and Taylor, {D. E.}",
year = "1993",
month = "1",
day = "1",
doi = "10.1128/AAC.37.12.2645",
language = "English (US)",
volume = "37",
pages = "2645--2649",
journal = "Antimicrobial Agents and Chemotherapy",
issn = "0066-4804",
publisher = "American Society for Microbiology",
number = "12",

}

TY - JOUR

T1 - Effect of mutational alteration of Asn-128 in the putative GTP-binding domain of tetracycline resistance determinant Tet(O) from Campylobacter jejuni

AU - Grewal, J.

AU - Manavathu, E. K.

AU - Taylor, D. E.

PY - 1993/1/1

Y1 - 1993/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0027504919&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027504919&partnerID=8YFLogxK

U2 - 10.1128/AAC.37.12.2645

DO - 10.1128/AAC.37.12.2645

M3 - Article

C2 - 8109930

AN - SCOPUS:0027504919

VL - 37

SP - 2645

EP - 2649

JO - Antimicrobial Agents and Chemotherapy

JF - Antimicrobial Agents and Chemotherapy

SN - 0066-4804

IS - 12

ER -