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.

Author: Bartsevich, Victor V., Shestakov, Sergey V.
Observations, Drug resistance in microorganisms, Microbial drug resistance

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


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.

Author: Malakhov, Michael P., Los, Dmitry A., Wada, Hajime, Semenenko, Victor E., Murata, Norio
Genetic aspects, Microbial mutation

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


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.

Author: Okumura, Noriko, Wada, Hajime, Masamoto, Kazumori
Glutathione metabolism

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Subjects list: Research, Analysis, Cyanobacteria, Amino acid sequence, Amino acid sequencing
This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.