DABs are inorganic carbon pumps found throughout prokaryotic phyla
| العنوان: | DABs are inorganic carbon pumps found throughout prokaryotic phyla |
|---|---|
| المؤلفون: | Thomas G. Laughlin, John J Desmarais, Joy Y. Wang, Allen W. Chen, Avi I. Flamholz, Kelly M. Wetmore, Luke M. Oltrogge, Spencer Diamond, Eli J Dugan, Cecilia Blikstad, David F. Savage |
| المصدر: | Nature microbiology, vol 4, iss 12 Nat Microbiol |
| بيانات النشر: | eScholarship, University of California, 2019. |
| سنة النشر: | 2019 |
| مصطلحات موضوعية: | Operon, medicine.disease_cause, Applied Microbiology and Biotechnology, Essential, Vibrio cholerae, Carbonic Anhydrases, 0303 health sciences, Genes, Essential, biology, Bacterial, Halothiobacillus, Infectious Diseases, Biochemistry, Medical Microbiology, Biotechnology, Microbiology (medical), Transposable element, 1.1 Normal biological development and functioning, Immunology, Sulfanilic Acids, Locus (genetics), Microbiology, Article, Vaccine Related, 03 medical and health sciences, Rare Diseases, Bacterial Proteins, Underpinning research, Biodefense, medicine, Genetics, Gene, 030304 developmental biology, Bacteria, 030306 microbiology, Phylum, Prevention, Cell Biology, Diazonium Compounds, Carbon Dioxide, biology.organism_classification, Archaea, Carbon, Bicarbonates, Emerging Infectious Diseases, Prokaryotic Cells, Genes, Genes, Bacterial, Mutagenesis, Bacillus anthracis, DNA Transposable Elements, Carrier Proteins |
| الوصف: | 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 β-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. |
| وصف الملف: | application/pdf |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da6741af8ff6acae75b17a234bc1911f https://escholarship.org/uc/item/31j2806m |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....da6741af8ff6acae75b17a234bc1911f |
| قاعدة البيانات: | OpenAIRE |
| الوصف غير متاح. |