Abstract
The gene encoding a cell division protein FtsZ1 was cloned from an extremely halophilic archaeon, Haloarcula japonica strain TR-1. Nucleotide sequencing analysis of the ftsZ1 gene revealed that the structural gene consisted of an open reading frame of 1,158 nucleotides encoding 386 amino acids. Transcription of the ftsZ1 gene in Ha. japonica was confirmed by RT-PCR. A modified ftsZ1 gene was inserted into the shuttle vector pWL102 and used to transform Ha. japonica. The recombinant FtsZ1 was produced as a fusion with hexahistidine-tag in Ha. japonica host cells and purified. Purified recombinant FtsZ1 exhibited GTP-dependent polymerization activity and GTP-hydrolyzing activity in the presence of high concentrations of KCl.
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