Disease relevance of ctpA

• We have recently identified a gene, ctpA, a mutation in which resulted in a loss of PSII activity in the cyanobacterium Synechocystis sp. PCC 6803 [1].
• The predicted sequence of the encoded protein showed significant similarity to that of the Prc protein, a carboxyl-terminal processing protease in Escherichia coli [2].

High impact information on ctpA

• The ctpA gene encodes the C-terminal processing protease for the D1 protein of the photosystem II reaction center complex [1].
• To study the function of the CtpA protein, we inactivated the ctpA gene by inserting a kanamycin-resistance gene into its coding sequence [1].
• Here, we studied the effect of ctpA gene inactivation on the B. burgdorferi protein expression profile [3].
• The ctpA gene does not directly affect the erythrocyte-invasion phenotype conferred by ialAB, but its homology to other stress-response processing proteases implies an important role in survival of this intracellular pathogen [4].
• The Synechocystis sp. PCC 6803 ctp gene family members ctpA (slr0008), ctpB (slr0257) and ctpC (slr1751), encoding carboxyl-terminal endoproteases (Ctps), were studied at levels of gene transcription and protein structure [5].

Analytical, diagnostic and therapeutic context of ctpA

• Molecular cloning and characterization of the ctpA gene encoding a carboxyl-terminal processing protease. Analysis of a spontaneous photosystem II-deficient mutant strain of the cyanobacterium Synechocystis sp. PCC 6803 [2].
• Total B. burgdorferi proteins were separated by two-dimensional gel electrophoresis, and the results revealed that six proteins of the wild type were not detected in the ctpA mutant and that nine proteins observed in the ctpA mutant were undetectable in the wild type [3].

References