Transcriptional regulation of acetyl CoA and lipid synthesis by P protein in Synechococcus PCC 7942.

P protein family is widespread in prokaryotes and plants. In this study, impacts of P deficiency on the synthesis of acetyl CoA and acetyl CoA carboxylase enzyme (ACCase) was analyzed in the Synechococcus sp. PCC 7942 by evaluating the mRNA levels of pyruvate kinase (PK), pyruvate dehydrogenase (PDH), citrate synthase (CS), biotin synthase (BS), biotin carboxylase (BC), biotin carboxyl carrier protein (BCCP), carboxyl transferase (CT) α and β subunits. The P deficient Synechococcus sp. PCC 7942 showed upregulation of all the above-mentioned genes, except CS. Analyses of genes required for acetyl coA synthesis exhibited a substantial increase in the transcript levels of PK and PDH in the P mutant strain. In addition, the P mutant also displayed reduced acetyl CoA content, high ACCase activity, and increased lipid content. The lessening of acetyl CoA content was attributed to the rapid utilization of acetyl CoA in fatty acid synthesis as well as in the TCA cycle whereas the increased ACCase activity was ascribed to the rise in mRNA levels of BS, BC, BCCP, CT α, and β genes. However, increased lipid content was correlated with the declined total protein content. Hence, the study suggested that P protein regulates the synthesis of acetyl CoA and ACCase enzyme at the transcriptional level.