Cloning and characterization of an ftsZ homologue from a bacterial symbiont of Drosophila melanogaster
| Autor: | John F. Y. Brookfield, Peter R. Holden, Peter B. Jones |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
DNA
Bacterial Cell division Molecular Sequence Data Bacillus subtilis Biology medicine.disease_cause Polymerase Chain Reaction Bacterial Proteins GTP-Binding Proteins RNA Ribosomal 16S Genetics medicine Animals Amino Acid Sequence Cloning Molecular FtsZ Symbiosis Molecular Biology Escherichia coli Peptide sequence Gene Rickettsieae Base Sequence Sequence Homology Amino Acid Nucleic acid sequence Tetracycline biology.organism_classification Blotting Southern Cytoskeletal Proteins RNA Bacterial Drosophila melanogaster Larva biology.protein bacteria |
| Zdroj: | Moleculargeneral genetics : MGG. 240(2) |
| ISSN: | 0026-8925 |
| Popis: | A 1194 bp open reading frame that codes for a 398 amino acid peptide was cloned from a lambda gt11 library of Drosophila melanogaster genomic DNA. The predicted peptide sequence is very similar to three previously characterized protein sequences that are encoded by the ftsZ genes in Escherichia coli, Bacillus subtilis and Rhizobium meliloti. The FtsZ protein has a major role in the initiation of cell division in prokaryotic cells. Using a tetracycline treatment that eradicates bacterial parasites from insects, the ftsZ homologue has been found to be derived from a bacterium that lives within the D. melanogaster strain. However, polymerase chain reaction (PCR) amplification of the gene from treated embryos suggests that it is not derived from a gut bacterium. Nevertheless, by amplifying and characterizing part of the 16S rRNA from this bacterium we have been able to demonstrate that it is a member of the genus Wolbachia, a parasitic organism that infects, and disturbs the sexual cycle of various strains of Drosophila simulans. We suggest that this ftsZ homologue is implicated in the cell division of Wolbachia, an organism that fails to grow outside the host organism. Sequence and alignment analysis of this ftsZ homologue show the presence of a potential GTP-binding motif indicating that it may function as a GTPase. The consequences of this function particularly with respect to its role in cell division are discussed. |
| Databáze: | OpenAIRE |
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