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Genome-wide screening reveals a novel class of carbonic anhydrase-like inorganic carbon transporters in chemoautotrophic bacteria

By John J Desmarais, Avi Flamholz, Cecilia Blikstad, Eli J Dugan, Thomas G Laughlin, Luke M Oltrogge, Allen W Chen, Kelly Wetmore, Spencer Diamond, Joy Y Wang, David Savage

Posted 22 Nov 2018
bioRxiv DOI: 10.1101/476713

Many bacterial autotrophs rely on CO2 concentrating mechanisms (CCMs) to assimilate carbon. Although many CCM proteins have been identified, including a 200+ MDa protein organelle called the carboxysome, a systematic screen of CCM components has not been carried out. Here, we performed a genome-wide barcoded transposon screen to identify essential and CCM-related genes in the γ-proteobacterium H. neapolitanus. Our screen revealed an operon critical for CCM function which encodes a domain of unknown function (PFAM:PF10070) and putative cation transporter subunit (PFAM:PF00361). These two proteins, which we name DabA and DabB for "DABs accumulate bicarbonate," function as a heterodimeric, energy-coupled inorganic carbon pump in E. coli. Furthermore, DabA binds zinc and has a an active site homologous to a β-carbonic anhydrase. Based on these results, we propose that DABs function as vectorial CAs coupled to cation gradients and serve as inorganic carbon pumps throughout prokaryotic phyla.

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