A parts list for fungal cellulosomes revealed by comparative genomics
| Autor: | Alan Kuo, Theo A. van Alen, Charles H. Haitjema, John K. Henske, Johannes H. P. Hackstein, Jennifer Chiniquy, Igor V. Grigoriev, Samuel O. Purvine, Randall de Groot, Kevin V. Solomon, Zhiying Zhao, Stephen J. Mondo, Kurt LaButti, Aaron T. Wright, Heather M. Brewer, Sean P. Gilmore, Kerrie Barry, Brigitte Boxma, Matthieu Hainaut, Bernard Henrissat, Scott E. Baker, Michelle A. O’Malley, Asaf Salamov |
|---|---|
| Přispěvatelé: | Department of Chemical Engineering, Department of chemical engineering, US Department of Energy, Joint Genome Institute (JGI), Environmental Molecular Sciences Laboratory, Earth and Biological Sciences Directorate, Pacific Northwest National Laboratory (PNNL), Biological Sciences Division, Earth and Biological Sciences Directorate, Architecture et fonction des macromolécules biologiques (AFMB), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Aix Marseille Université (AMU), Institut National de la Recherche Agronomique (INRA), Department of Evolutionary Microbiology, Radboud University Nijmegen, Department of Biological Sciences, The Open University [Milton Keynes] (OU), Department of Plant and Microbial Biology, US Department of Energy (DE-SC0010352), the US Department of Agriculture (award no. 2011-67017-20459), the National Science Foundation (DGE 1144085), W911NF-09-0001 (FICUS), DE-AC02-05CH11231 (JGI)DE-AC05-76RL01830 (EMSL).IDEX Aix-Marseille (Grant Microbio-E) (grant no. ANR-14-CE06-0020), Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA) |
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Proteomics [SDV]Life Sciences [q-bio] Neocallimastigales microbiome Dockerin approche protéomique Applied Microbiology and Biotechnology Cellulosome assembly Cellulosome Fungal genetics neocallimastix 2.2 Factors relating to the physical environment Aetiology biology Genomics Cellulosomes Infectious Diseases Medical Microbiology fungal genome anaeromyces Piromyces Anaerobic bacteria génome fongique Infection Biotechnology Protein Binding Microbiology (medical) 030106 microbiology Immunology Multienzyme complexes Computational biology Microbiology Fungal Proteins 03 medical and health sciences Genetics analyse génomique biomasse végétale Comparative genomics Cell Biology biology.organism_classification piromyces 030104 developmental biology Neocallimastigomycota cellulosome Ecological Microbiology génie génétique Protein Multimerization |
| Zdroj: | Nature Microbiology Nature Microbiology, 2017, 2, pp.17087. ⟨10.1038/nmicrobiol.2017.87⟩ Nature Microbiology, Nature Publishing Group, 2017, 2, pp.17087. ⟨10.1038/nmicrobiol.2017.87⟩ Nature microbiology, vol 2, iss 8 Nature Microbiology, 2, pp. 1-8 Haitjema, CH; Gilmore, SP; Henske, JK; Solomon, KV; De Groot, R; Kuo, A; et al.(2017). A parts list for fungal cellulosomes revealed by comparative genomics. Nature Microbiology, 2. doi: 10.1038/nmicrobiol.2017.87. Lawrence Berkeley National Laboratory: Retrieved from: http://www.escholarship.org/uc/item/6d7283vx Nature Microbiology, 2, 1-8 |
| ISSN: | 2058-5276 |
| DOI: | 10.1038/nmicrobiol.2017.87⟩ |
| Popis: | © 2017 Macmillan Publishers Limited, part of Springer Nature. All rights reserved. Cellulosomes are large, multiprotein complexes that tether plant biomass-degrading enzymes together for improved hydrolysis1. These complexes were first described in anaerobic bacteria, where species-specific dockerin domains mediate the assembly of enzymes onto cohesin motifs interspersed within protein scaffolds 1. The versatile protein assembly mechanism conferred by the bacterial cohesin-dockerin interaction is now a standard design principle for synthetic biology2,3. For decades, analogous structures have been reported in anaerobic fungi, which are known to assemble by sequence-divergent non-catalytic dockerin domains (NCDDs)4. However, the components, modular assembly mechanism and functional role of fungal cellulosomes remain unknown5,6. Here, we describe a comprehensive set of proteins critical to fungal cellulosome assembly, including conserved scaffolding proteins unique to the Neocallimastigomycota. High-quality genomes of the anaerobic fungi Anaeromyces robustus, Neocallimastix californiae and Piromyces finnis were assembled with long-read, single-molecule technology. Genomic analysis coupled with proteomic validation revealed an average of 312 NCDD-containing proteins per fungal strain, which were overwhelmingly carbohydrate active enzymes (CAZymes), with 95 large fungal scaffoldins identified across four genera that bind to NCDDs. Fungal dockerin and scaffoldin domains have no similarity to their bacterial counterparts, yet several catalytic domains originated via horizontal gene transfer with gut bacteria. However, the biocatalytic activity of anaerobic fungal cellulosomes is expanded by the inclusion of GH3, GH6 and GH45 enzymes. These findings suggest that the fungal cellulosome is an evolutionarily chimaeric structure - an independently evolved fungal complex that co-opted useful activities from bacterial neighbours within the gut microbiome. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|