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EFFECT OF MUTATIONAL ALTERATION OF ASN-128 IN THE PUTATIVE GTP-BINDING DOMAIN OF TETRACYCLINE RESISTANCE DETERMINANT TET(O) FROM CAMPYLOBACTER-JEJUNI
被引：14
|作者：
GREWAL, J
MANAVATHU, EK
TAYLOR, DE
机构：
[1] UNIV ALBERTA,DEPT MED MICROBIOL & INFECT DIS,EDMONTON T6G 2H7,AB,CANADA
[2] WAYNE STATE UNIV,DEPT INTERNAL MED,DIV INFECT DIS,DETROIT,MI 48201
关键词：
D O I：
10.1128/AAC.37.12.2645
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ;
100705 ;
摘要：
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-Tn-GDP complex as a model.
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页码：2645 / 2649
页数：5
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