Cloning and organization of the abc and mdl genes of Escherichia coli: relationship to eukaryotic multidrug resistance
| Autor: | Bernard Gerrard, Michael Dean, Rando Allikmets, Don Court |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
DNA
Bacterial Subfamily Molecular Sequence Data ATP-binding cassette transporter Biology medicine.disease_cause Adenosine Triphosphate Bacterial Proteins Escherichia coli Genetics medicine Humans Gene family ATP Binding Cassette Transporter Subfamily B Member 1 Amino Acid Sequence Cloning Molecular Gene Membrane Glycoproteins Base Sequence Permease Escherichia coli Proteins Nucleic acid sequence Chromosome Mapping Membrane Proteins Drug Resistance Microbial General Medicine Open reading frame Genes Bacterial ATP-Binding Cassette Transporters Carrier Proteins |
| Zdroj: | Gene. 136:231-236 |
| ISSN: | 0378-1119 |
| DOI: | 10.1016/0378-1119(93)90470-n |
| Popis: | 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- l ike), 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 . Genedisruption studies revealed that mdl is not essential for cell growth. The second open reading frame, named abc ( ATP-b nding 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. |
| Databáze: | OpenAIRE |
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