DABs are inorganic carbon pumps found throughout prokaryotic phyla.
Nat Microbiol
; 4(12): 2204-2215, 2019 12.
Article
em En
| MEDLINE
| ID: mdl-31406332
ABSTRACT
Bacterial autotrophs often rely on CO2 concentrating mechanisms (CCMs) to assimilate carbon. Although many CCM proteins have been identified, a systematic screen of the components of CCMs is lacking. Here, we performed a genome-wide barcoded transposon screen to identify essential and CCM-related genes in the γ-proteobacterium Halothiobacillus neapolitanus. Screening revealed that the CCM comprises at least 17 and probably no more than 25 genes, most of which are encoded in 3 operons. Two of these operons (DAB1 and DAB2) contain a two-gene locus that encodes a domain of unknown function (Pfam PF10070) and a putative cation transporter (Pfam PF00361). Physiological and biochemical assays demonstrated that these proteins-which we name DabA and DabB, for DABs accumulate bicarbonate-assemble into a heterodimeric complex, which contains a putative ß-carbonic anhydrase-like active site and functions as an energy-coupled inorganic carbon (Ci) pump. Interestingly, DAB operons are found in a diverse range of bacteria and archaea. We demonstrate that functional DABs are present in the human pathogens Bacillus anthracis and Vibrio cholerae. On the basis of these results, we propose that DABs constitute a class of energized Ci pumps and play a critical role in the metabolism of Ci throughout prokaryotic phyla.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Células Procarióticas
/
Proteínas de Bactérias
/
Carbono
/
Proteínas de Transporte
/
Anidrases Carbônicas
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article