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PMID:7689140

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Citation

Holden, PR, Brookfield, JF and Jones, P (1993) Cloning and characterization of an ftsZ homologue from a bacterial symbiont of Drosophila melanogaster. Mol. Gen. Genet. 240:213-20

Abstract

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.

Links

PubMed

Keywords

Amino Acid Sequence; Animals; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Base Sequence; Blotting, Southern; Cloning, Molecular; Cytoskeletal Proteins; DNA, Bacterial; Drosophila melanogaster/microbiology; GTP-Binding Proteins/genetics; GTP-Binding Proteins/metabolism; Larva; Molecular Sequence Data; Polymerase Chain Reaction; RNA, Bacterial/genetics; RNA, Ribosomal, 16S/genetics; Rickettsieae/genetics; Rickettsieae/metabolism; Rickettsieae/physiology; Sequence Homology, Amino Acid; Symbiosis; Tetracycline/pharmacology

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

WOLSP:FTSZ

GO:0051301: cell division

ECO:0000247:

UniProtKB:P0A9A6


P

Fig 3. In E.coli K12, ftsZ functions in cell division inferred from mutant phenotype PubMed 2045370. Source: EcoliWiki

complete
CACAO 8234

WOLSP:FTSZ

GO:0005737: cytoplasm

ECO:0000247:

UniProtKB:P0A9A6


C

Fig 3. In E.coli K12, ftsZ is located in cytoplasm inferred from direct assay PubMed 1943703. Source: EcoliWiki

complete
CACAO 8235

WOLSP:FTSZ

GO:0005525: GTP binding

ECO:0000247:

UniProtKB:P0A9A6


F

Fig 3. In E.coli K12, ftsZ has GTP binding activity inferred from direct assay PMID:1528267[1] PMID:1528268[2] . Source: EcoliWiki

complete
CACAO 8236

WOLSP:FTSZ

GO:0051258: protein polymerization

ECO:0000247:

UniProtKB:P0A9A6


P

Fig 3. In E.coli K12, ftsZ functions in protein polymerization inferred from direct assay PubMed 21321206 and PubMed 8917533 Source: EcoliWiki

complete
CACAO 8237

WOLSP:FTSZ

enables

GO:0005525: GTP binding

ECO:0000247: sequence alignment evidence used in manual assertion

UniProtKB:P0A9A6

F

Seeded From UniProt

complete


See also

References

See Help:References for how to manage references in GONUTS.

  1. RayChaudhuri, D & Park, JT (1992) Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein. Nature 359 251-4 PubMed GONUTS page
  2. de Boer, P et al. (1992) The essential bacterial cell-division protein FtsZ is a GTPase. Nature 359 254-6 PubMed GONUTS page