Complete nucleotide sequence of phoE, the structural gene for the phosphate limitation inducible outer membrane pore protein of Escherichia coli K12
| Autor: | Ben J. J. Lugtenberg, Hans Bergmans, Nico Overbeeke, Fons van Mansfeld |
|---|---|
| Rok vydání: | 1983 |
| Předmět: |
Signal peptide
Transcription Genetic Deoxyribonucleotides Peptide Biology medicine.disease_cause Bacterial Proteins Structural Biology Genes Regulator medicine Consensus sequence Escherichia coli Amino Acid Sequence Molecular Biology Peptide sequence chemistry.chemical_classification Base Sequence Structural gene Nucleic acid sequence Chromosome Mapping Membrane Proteins Amino acid chemistry Biochemistry Genes Electrophoresis Polyacrylamide Gel Bacterial Outer Membrane Proteins Plasmids |
| Zdroj: | Journal of molecular biology. 163(4) |
| ISSN: | 0022-2836 |
| Popis: | The complete nucleotide sequence of the gene phoE, which codes for the phosphate limitation inducible outer membrane pore protein of Escherichia coli K12 was established. The results show that PhoE protein is synthesized in a precursor form with a 21 amino acid residue amino-terminal extension. This peptide has the general characteristics of a signal sequence. The promoter region of phoE has no homlogy with the consensus sequence of E. coli promoter regions, but homologous sequences with the promoter region of phoA, the structural gene for alkaline phosphatase, were observed. The deduced amino acid sequence showed that the mature PhoE protein is composed of 330 amino acid residues with a calculated molecular weight of 36,782. A number of 81 charged amino acids was found scattered throughout the protein while no large stretches of hydrophobic amino acids were observed. Hydrophobicity and hydration profiles of PhoE protein showed five pronounced hydrophilic maxima which are all located in the region from the amino terminus to residue 212. When the deduced amino acid sequence of PhoE protein was compared with the established sequence of the OmpF pore protein, a number of 210 identical residues was found. Some aspects of the structure-function relationship of PhoE protein are discussed in view of the hydrophobicity and hydration profiles, and the homology between PhoE protein and OmpF protein. |
| Databáze: | OpenAIRE |
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