Genes encoding two lipoproteins in the leuS-dacA region of the Escherichia coli chromosome
| Autor: | S Asoh, Michio Matsuhashi, H Kamata, Fumitoshi Ishino, M. Doi, I Takase, Hiroshi Matsuzawa, Takahisa Ohta, Masaaki Wachi |
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| Rok vydání: | 1987 |
| Předmět: |
DNA
Bacterial Signal peptide Lipoproteins Molecular Sequence Data Protein Sorting Signals Biology medicine.disease_cause Microbiology Bacterial Proteins Escherichia coli medicine Amino Acid Sequence Cloning Molecular Molecular Biology Peptide sequence Gene Gel electrophoresis chemistry.chemical_classification Signal peptidase Base Sequence Chromosomes Bacterial Molecular biology Anti-Bacterial Agents Amino acid chemistry Biochemistry Genes Bacterial Electrophoresis Polyacrylamide Gel lipids (amino acids peptides and proteins) Peptides Plasmids Research Article Lipoprotein |
| Zdroj: | Journal of Bacteriology. 169:5692-5699 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.169.12.5692-5699.1987 |
| Popis: | The coding of two rare lipoproteins by two genes, rlpA and rlpB, located in the leuS-dacA region (15 min) on the Escherichia coli chromosome was demonstrated by expression of subcloned genes in a maxicell system. The formation of these two proteins was inhibited by globomycin, which is an inhibitor of the signal peptidase for the known lipoproteins of E. coli. In each case, this inhibition was accompanied by formation of a new protein, which showed a slightly lower mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and which we suppose to be a prolipoprotein with an N-terminal signal peptide sequence similar to those of the bacterial major lipoproteins and lysis proteins of some bacteriocins. The incorporation of 3H-labeled palmitate and glycerol into the two lipoproteins was also observed. Sequencing of DNA showed that the two lipoprotein genes contained sequences that could code for signal peptide sequences of 17 amino acids (rlpA lipoprotein) and 18 amino acids (rlpB lipoprotein). The deduced sequences of the mature peptides consisted of 345 amino acids (Mr 35,614, rlpA lipoprotein) and 175 amino acids (Mr 19,445, rlpB lipoprotein), with an N-terminal cysteine to which thioglyceride and N-fatty acyl residues may be attached. These two lipoproteins may be important in duplication of the cells. |
| Databáze: | OpenAIRE |
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