DesC1 and DesC2, Δ9 Fatty Acid Desaturases of Filamentous Cyanobacteria: Essentiality and Complementarity

• Published in: Plant And Cell Physiology
• Main Authors: Effendi, Devi B, Suzuki, Iwane, Murata, Norio, Awai, Koichiro
• Other Authors: Japan Society for the Promotion of Science
• Format: Article in Journal/Newspaper
• Language: English
• Published: Oxford University Press (OUP) 2023
• Subjects: Antarc*; Antarctic
• Online Access: http://dx.doi.org/10.1093/pcp/pcad153; https://academic.oup.com/pcp/advance-article-pdf/doi/10.1093/pcp/pcad153/54878747/pcad153.pdf; https://academic.oup.com/pcp/article-pdf/65/6/975/58345658/pcad153.pdf

Abstract DesC1 and DesC2, which are fatty acid desaturases found in cyanobacteria, are responsible for introducing a double bond at the Δ9 position of fatty-acyl chains, which are subsequently esterified to the sn-1 and sn-2 positions of the glycerol moiety, respectively. However, since the discovery of these two desaturases in the Antarctic cyanobacterium Nostoc sp. SO-36, no further research has been reported. This study presents a comprehensive characterization of DesC1 and DesC2 through targeted mutagenesis and transformation using two cyanobacteria strains: Anabaena sp. PCC 7120, comprising both desaturases, and Synechocystis sp. PCC 6803, containing a single Δ9 desaturase (hereafter referred to as DesCs) sharing similarity with DesC1 in amino acid sequence. The results suggested that both DesC1 and DesC2 were essential in Anabaena sp. PCC 7120 and that DesC1, but not DesC2, complemented DesCs in Synechocystis sp. PCC 6803. In addition, DesC2 from Anabaena sp. PCC 7120 desaturated fatty acids esterified to the sn-2 position of the glycerol moiety in Synechocystis sp. PCC 6803.