Cargando…
A Biological Nanomachine at Work: Watching the Cellulosome Degrade Crystalline Cellulose
[Image: see text] The cellulosome is a supramolecular multienzymatic protein complex that functions as a biological nanomachine of cellulosic biomass degradation. How the megadalton-size cellulosome adapts to a solid substrate is central to its mechanism of action and is also key for its efficient u...
Autores principales: | , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2020
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7256933/ https://www.ncbi.nlm.nih.gov/pubmed/32490190 http://dx.doi.org/10.1021/acscentsci.0c00050 |
_version_ | 1783540019816824832 |
---|---|
author | Eibinger, Manuel Ganner, Thomas Plank, Harald Nidetzky, Bernd |
author_facet | Eibinger, Manuel Ganner, Thomas Plank, Harald Nidetzky, Bernd |
author_sort | Eibinger, Manuel |
collection | PubMed |
description | [Image: see text] The cellulosome is a supramolecular multienzymatic protein complex that functions as a biological nanomachine of cellulosic biomass degradation. How the megadalton-size cellulosome adapts to a solid substrate is central to its mechanism of action and is also key for its efficient use in bioconversion applications. We report time-lapse visualization of crystalline cellulose degradation by individual cellulosomes from Clostridium thermocellum by atomic force microscopy. Upon binding to cellulose, the cellulosomes switch to elongated, even filamentous shapes and morph these dynamically at below 1 min time scale according to requirements of the substrate surface under attack. Compared with noncomplexed cellulases that peel off material while sliding along crystalline cellulose surfaces, the cellulosomes remain bound locally for minutes and remove the material lying underneath. The consequent roughening up of the surface leads to an efficient deconstruction of cellulose nanocrystals both from the ends and through fissions within. Distinct modes of cellulose nanocrystal deconstruction by nature’s major cellulase systems are thus revealed. |
format | Online Article Text |
id | pubmed-7256933 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-72569332020-06-01 A Biological Nanomachine at Work: Watching the Cellulosome Degrade Crystalline Cellulose Eibinger, Manuel Ganner, Thomas Plank, Harald Nidetzky, Bernd ACS Cent Sci [Image: see text] The cellulosome is a supramolecular multienzymatic protein complex that functions as a biological nanomachine of cellulosic biomass degradation. How the megadalton-size cellulosome adapts to a solid substrate is central to its mechanism of action and is also key for its efficient use in bioconversion applications. We report time-lapse visualization of crystalline cellulose degradation by individual cellulosomes from Clostridium thermocellum by atomic force microscopy. Upon binding to cellulose, the cellulosomes switch to elongated, even filamentous shapes and morph these dynamically at below 1 min time scale according to requirements of the substrate surface under attack. Compared with noncomplexed cellulases that peel off material while sliding along crystalline cellulose surfaces, the cellulosomes remain bound locally for minutes and remove the material lying underneath. The consequent roughening up of the surface leads to an efficient deconstruction of cellulose nanocrystals both from the ends and through fissions within. Distinct modes of cellulose nanocrystal deconstruction by nature’s major cellulase systems are thus revealed. American Chemical Society 2020-05-06 2020-05-27 /pmc/articles/PMC7256933/ /pubmed/32490190 http://dx.doi.org/10.1021/acscentsci.0c00050 Text en Copyright © 2020 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes. |
spellingShingle | Eibinger, Manuel Ganner, Thomas Plank, Harald Nidetzky, Bernd A Biological Nanomachine at Work: Watching the Cellulosome Degrade Crystalline Cellulose |
title | A Biological Nanomachine at Work: Watching the Cellulosome
Degrade Crystalline Cellulose |
title_full | A Biological Nanomachine at Work: Watching the Cellulosome
Degrade Crystalline Cellulose |
title_fullStr | A Biological Nanomachine at Work: Watching the Cellulosome
Degrade Crystalline Cellulose |
title_full_unstemmed | A Biological Nanomachine at Work: Watching the Cellulosome
Degrade Crystalline Cellulose |
title_short | A Biological Nanomachine at Work: Watching the Cellulosome
Degrade Crystalline Cellulose |
title_sort | biological nanomachine at work: watching the cellulosome
degrade crystalline cellulose |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7256933/ https://www.ncbi.nlm.nih.gov/pubmed/32490190 http://dx.doi.org/10.1021/acscentsci.0c00050 |
work_keys_str_mv | AT eibingermanuel abiologicalnanomachineatworkwatchingthecellulosomedegradecrystallinecellulose AT gannerthomas abiologicalnanomachineatworkwatchingthecellulosomedegradecrystallinecellulose AT plankharald abiologicalnanomachineatworkwatchingthecellulosomedegradecrystallinecellulose AT nidetzkybernd abiologicalnanomachineatworkwatchingthecellulosomedegradecrystallinecellulose AT eibingermanuel biologicalnanomachineatworkwatchingthecellulosomedegradecrystallinecellulose AT gannerthomas biologicalnanomachineatworkwatchingthecellulosomedegradecrystallinecellulose AT plankharald biologicalnanomachineatworkwatchingthecellulosomedegradecrystallinecellulose AT nidetzkybernd biologicalnanomachineatworkwatchingthecellulosomedegradecrystallinecellulose |