PMID:7904973
| Citation |
Allikmets, R, Gerrard, B, Court, D and Dean, M (1993) Cloning and organization of the abc and mdl genes of Escherichia coli: relationship to eukaryotic multidrug resistance. Gene 136:231-6 |
|---|---|
| Abstract |
Using degenerate oligodeoxyribonucleotides from conserved regions of the gene family encoding ATP-binding domain of the active transporter, two new Escherichia coli genes were identified. The first of the genes, named mdl (multidrug resistance-like), is located at min 10.2 of the E. coli chromosome and encodes two ATP-binding motifs and two hydrophobic (transmembrane) domains. The ATP-binding domains of mdl show 35-38% amino acid (aa) identity with members of the eukaryotic P-glycoprotein/multidrug resistance family. To date, 25 members of the ATP-transporter/permease gene family have been characterized in E. coli. Comparison of the ATP-binding domains from this family indicates that mdl is part of a distinct subfamily of sequences that includes hlyB, msbA, and cvaB. Gene-disruption studies revealed that mdl is not essential for cell growth. The second open reading frame, named abc (ATP-binding cassette), is located at min 4.9 of the chromosome, encodes a single ATP-binding domain, and is most homologous to ftsE, a cell division control gene of E. coli. The abc gene product also shows aa sequence homology to several E. coli permeases. |
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| Keywords |
ATP-Binding Cassette Transporters; Adenosine Triphosphate; Amino Acid Sequence; Bacterial Proteins/genetics; Base Sequence; Carrier Proteins/genetics; Chromosome Mapping; Cloning, Molecular; DNA, Bacterial; Drug Resistance, Microbial/genetics; Escherichia coli/drug effects; Escherichia coli/genetics; Escherichia coli Proteins; Genes, Bacterial; Humans; Membrane Glycoproteins/genetics; Membrane Proteins/genetics; Molecular Sequence Data; P-Glycoprotein |
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