The dspA gene product of the cyanobacterium Synechocystis sp. strain PCC 6803 influences sensitivity to chemically different growth inhibitors and has amino acid similarity to histidine protein kinases
Article Abstract:
The dspA gene of the cyanobacteria Synechocystis sp. strain PCC 6803 controls sensitivity to the herbicides, difunon and diuron, chlorpromazine and trifluoperazine. Mutations in dspA make the bacteria resistant to these compounds. The dspA gene encodes the drug sensory protein A (DspA) which contains 663 amino acids with a molecular mass of 74.5 kDa. The N- and C-terminal of DspA are structurally similar to the conserved sequence of histidine protein kinases (HPKs). DspA is a sensory HPK probably involved in the sensing chemical compounds.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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Characterization of the murF gene of the cyanobacterium Synechocystis sp. PCC 6803
Article Abstract:
The murF gene from the cyanobacterium Synechocystis sp.PCC 6803 codes for a 48 kDa polypeptide with 454 amino acid residues. The single copy gene in the Synechocystis genome exhibits 39% identity with the amino acid sequence of the murF gene product of Escherichia coli. The murF-deficient E. coli strain regains its cell wall-synthesizing and high sublethal-temperature-surviving capacity when its temperature-responsive mutation is complemented by the cyanobacterial murF gene.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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The gshB gene in the cyanobacterium Synechococcus sp. PCC 7942 encodes a functional glutathione synthetase
Article Abstract:
A study was conducted on the gshB gene to determine its role in the biosynthesis of glutathione in the Synnechococcus sp. PCC 7942 cyanobacterium. The gshB was cloned from genomic DNA library to the wild-type cyanobacterium using the Southern blot analysis with the plasmid rescued from mutant strain NOK-1 as a probe. Results have shown that the glutathione synthetase activity significantly increased when the gshB was overexpressed in Escherichia coli.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
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