Disease relevance of desA

• The primary signal in the biological perception of temperature: Pd-catalyzed hydrogenation of membrane lipids stimulated the expression of the desA gene in Synechocystis PCC6803 [1].
• The transformation of Synechococcus PCC7942 with the desA genes from Synechocystis PCC6714, Synechococcus PCC7002 and A. variabilis was associated with the ability to introduce a second double bond at the delta 12 position of fatty acids [2].
• The desA gene for the delta 12 acyl-lipid desaturase was modified by site-directed mutagenesis, such that four of the histidine residues that are conserved in the four desaturases and one histidine residue that is not conserved were replaced by arginine, and the mutated desA genes were overexpressed in Escherichia coli [3].
• Cyanobacterial genes for enzymes that desaturate fatty acids at the delta 12 position, designated desA, were isolated from Synechocystis PCC6714, Synechococcus PCC7002 and Anabaena variabilis by cross-hybridization with a DNA probe derived from the desA gene of Synechocystis PCC6803 [2].

High impact information on desA

• The desA, desB and desD genes of Synechocystis sp. PCC 6803 encode acyl-lipid desaturases that introduce double bonds at the delta12, omega3 and delta6 positions of C18 fatty acids respectively [4].
• Bioenergetic responses of Synechocystis 6803 fatty acid desaturase mutants at low temperatures [5].
• The amino acid sequence of the products of the desA genes revealed the presence of four conserved domains [2].

Anatomical context of desA

• The Pd-catalyzed hydrogenation of plasma membrane lipids stimulated the expression of the desA gene [1].

Associations of desA with chemical compounds

• Rifampicin, chloramphenicol, and 3-(3, 4-dichlorophenyl)-1,1-dimethylurea completely blocked the induction of the expression of desA, desB, and desD [6].

References