The ftsZ gene of Haloferax mediterranei: sequence, conserved gene order, and visualization of the FtsZ ring.
We sequenced the ftsZ gene region of the halophilic archaeon Haloferax mediterranei and mapped the transcription start sites for the ftsZ gene. The gene encoded a 363-amino-acid long FtsZ protein with a predicted molecular mass of 38 kDa and an isoelectric point of 4.2. A high level of similarity to the FtsZ protein of Haloferax volcanii was apparent, with 97 and 90% identity at the amino acid and nucleotide levels, respectively. Structural conservation at the protein level was shown by visualization of the FtsZ ring structure in H. mediterranei cells using an antiserum raised against FtsZ of H. volcanii. FtsZ rings were observed in cells in different stages of division, including cells with pleomorphic shapes and cells that appeared to be undergoing asymmetric division. Cells were also observed that displayed constriction-like invaginations in the absence of an FtsZ ring, indicating that morphological data are not sufficient to determine whether pleomorphic Haloferax cells are undergoing cell division. Both the upstream and downstream gene order in the ftsZ region was found to be conserved within the genus Haloferax. Furthermore, the downstream gene order, which includes the secE and nusG genes, is conserved in almost all euryarchaea sequenced to date. The secE and nusG genes are likely to be transcriptionally and translationally coupled in Haloferax, and this co-expression may have been a selective force that has contributed to keeping the gene cluster intact.
Poplawski
A
A
Department of Cell and Molecular Biology, Biomedical Center, Uppsala University, Sweden.
Gullbrand
B
B
Bernander
R
R
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics*; D001483:Base Sequence; D017124:Conserved Sequence; D003598:Cytoskeletal Proteins; D004269:DNA, Bacterial / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D029968:Escherichia coli Proteins; D005455:Fluorescent Antibody Technique; D019621:Haloferax / Q000235:genetics; D019623:Haloferax mediterranei / Q000235:genetics*; D008856:Microscopy, Fluorescence; D008969:Molecular Sequence Data; D016366:Open Reading Frames / Q000235:genetics; D010445:Peptide Elongation Factors / Q000235:genetics; D000069816:SEC Translocation Channels; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors / Q000235:genetics
D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; D004269:DNA, Bacterial; D029968:Escherichia coli Proteins; C071525:FtsZ protein, Bacteria; C070291:NusG protein, E coli; D010445:Peptide Elongation Factors; D000069816:SEC Translocation Channels; C065493:SecE protein, E coli; D014157:Transcription Factors