Functional and structural analysis of carbonic anhydrases from the filamentous ascomycete Sordaria macrospora

TL;DRAbstract

Carbonic anhydrases (CAs) are metalloenzymes catalyzing the rapid and reversible hydration of carbon dioxide to bicarbonate (hydrogen carbonate) and protons. CAs have been identified in archaea, bacteria and eukaryotes and can be classified into five groups (α, β, γ, δ, ζ) that are unrelated in sequence and structure. The filamentous ascomycete Sordaria macrospora encodes four CAs, three of the β-class (cas1, cas2 and cas3) and one of the α-class (cas4). The CAS4 protein exhibits a functional N-terminal signal peptide for translocation into the endoplasmic reticulum and is posttranslationally glycosylated and targeted to the supernatant. The knockout strain Δcas4 had a significantly reduced rate of ascospore germination but showed no significant involvement into sexual development and vegetative growth. Vegetative growth rate of the quadruple mutant lacking all cas genes was drastically reduced compared to the wild type and the mutant invaded the agar under normal air conditions. Likew

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