A third periplasmic transport system for l-arginine in Escherichia coli: molecular characterization of the artPIQMJ genes, arginine binding and transport
| Autor: | Ternes D, S. Six, Johannes Bongaerts, S. Steinwachs, Gottfried Unden, Wissenbach U |
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| Rok vydání: | 1995 |
| Předmět: |
Signal peptide
Arginine Molecular Sequence Data Restriction Mapping Biology Cell Fractionation medicine.disease_cause Microbiology Bacterial Proteins Escherichia coli medicine Amino Acid Sequence Cloning Molecular Promoter Regions Genetic Molecular Biology chemistry.chemical_classification Genomic Library Arginine transport Base Sequence Sequence Homology Amino Acid Escherichia coli Proteins Membrane Proteins Biological Transport Periplasmic space Molecular biology Cell Compartmentation Amino acid chemistry Biochemistry Genes Bacterial Periplasmic Binding Proteins Amino Acid Transport Systems Basic Carrier Proteins Arginine binding Sequence Analysis |
| Zdroj: | Molecular Microbiology. 17:675-686 |
| ISSN: | 1365-2958 0950-382X |
| Popis: | A new binding-protein-dependent transport system of Escherichia coli specific for L-arginine was characterized by genetic and biochemical means. The system is encoded by five adjacent genes, artPIQMJ (art standing for arginine transport), which are organized in two transcriptional units (artPIQM and artJ). The artl and artJ gene products (Artl and ArtJ) are periplasmic binding proteins with sequence similarity to binding proteins for polar (basic) amino acids. The artQ, artM and artP products are similar to the transmembraneous proteins and the ATPase of binding-protein-dependent carriers. The mature Artl and J proteins were localized in the periplasm and lacked signal peptides of 19 amino acid residues. Artl and ArtJ were isolated from overproducing strains. ArtJ specifically binds L-arginine with high affinity and overproduction of ArtJ stimulated L-arginine uptake by the bacteria. The substrate for Artl is not known, and isolated Artl did not bind common amino acids, various basic uncommon amino acids or amines. It is concluded that the artPIQM artJ genes encode a third arginine-uptake system in addition to the known argT hisJQMP system of Salmonella typhimurium and E. coli and the arginine (-ornithine) carrier (aps) of E. coli. |
| Databáze: | OpenAIRE |
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