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Revealing Nature's Cellulase Diversity: The Digestion Mechanism of Caldicellulosiruptor bescii CelA.

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Title: Revealing Nature's Cellulase Diversity: The Digestion Mechanism of Caldicellulosiruptor bescii CelA.
Authors: Brunecky, Roman (AUTHOR), Alahuhta, Markus (AUTHOR), Qi Xu (AUTHOR), Donohoe, Bryon S. (AUTHOR), Crowley, Michael F. (AUTHOR), Kataeva, Irina A. (AUTHOR), Sung-Jae Yang (AUTHOR), Resch, Michael G. (AUTHOR), Adams, Michael W. W. (AUTHOR), Lunin, Vladimir V. (AUTHOR), Himmel, Michael E. (AUTHOR), Bomble, Yannick J. (AUTHOR)
Source: Science (pre-March 2025). 12/20/2013, Vol. 342 Issue 6165, p1513-1516. 4p.
Subjects: Cellulose, Cellulosomes, Thermophilic bacteria, Bacterial secretions, Exoglucanase, Transmission electron microscopy, Cellulose digestion
Abstract: Most fungi and bacteria degrade plant cell walls by secreting free, complementary enzymes that hydrolyze cellulose; however, some bacteria use large enzymatic assemblies called cellulosomes, which recruit complementary enzymes to protein scaffolds. The thermophilic bacterium Caldicellulosiruptor bescii uses an intermediate strategy, secreting many free cellulases that contain multiple catalytic domains. One of these, CelA, comprises a glycoside hydrolase family 9 and a family 48 catalytic domain, as well as three type III cellulose-binding modules. In the saccharification of a common cellulose standard, Avicel, CelA outperforms mixtures of commercially relevant exo- and endoglucanases. From transmission electron microscopy studies of cellulose after incubation with CelA, we report morphological features that suggest that CelA not only exploits the common surface ablation mechanism driven by general cellulase processivity, but also excavates extensive cavities into the surface of the substrate. These results suggest that nature's repertoire of cellulose digestion paradigms remain only partially discovered and understood. [ABSTRACT FROM AUTHOR]
Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Psychology and Behavioral Sciences Collection
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  Data: Revealing Nature's Cellulase Diversity: The Digestion Mechanism of Caldicellulosiruptor bescii CelA.
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  Data: <searchLink fieldCode="AR" term="%22Brunecky%2C+Roman%22">Brunecky, Roman</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Alahuhta%2C+Markus%22">Alahuhta, Markus</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Qi+Xu%22">Qi Xu</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Donohoe%2C+Bryon+S%2E%22">Donohoe, Bryon S.</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Crowley%2C+Michael+F%2E%22">Crowley, Michael F.</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Kataeva%2C+Irina+A%2E%22">Kataeva, Irina A.</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Sung-Jae+Yang%22">Sung-Jae Yang</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Resch%2C+Michael+G%2E%22">Resch, Michael G.</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Adams%2C+Michael+W%2E+W%2E%22">Adams, Michael W. W.</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Lunin%2C+Vladimir+V%2E%22">Lunin, Vladimir V.</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Himmel%2C+Michael+E%2E%22">Himmel, Michael E.</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Bomble%2C+Yannick+J%2E%22">Bomble, Yannick J.</searchLink> (AUTHOR)
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  Data: <searchLink fieldCode="JN" term="%22Science+%28pre-March+2025%29%22">Science (pre-March 2025)</searchLink>. 12/20/2013, Vol. 342 Issue 6165, p1513-1516. 4p.
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  Data: <searchLink fieldCode="DE" term="%22Cellulose%22">Cellulose</searchLink><br /><searchLink fieldCode="DE" term="%22Cellulosomes%22">Cellulosomes</searchLink><br /><searchLink fieldCode="DE" term="%22Thermophilic+bacteria%22">Thermophilic bacteria</searchLink><br /><searchLink fieldCode="DE" term="%22Bacterial+secretions%22">Bacterial secretions</searchLink><br /><searchLink fieldCode="DE" term="%22Exoglucanase%22">Exoglucanase</searchLink><br /><searchLink fieldCode="DE" term="%22Transmission+electron+microscopy%22">Transmission electron microscopy</searchLink><br /><searchLink fieldCode="DE" term="%22Cellulose+digestion%22">Cellulose digestion</searchLink>
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  Data: Most fungi and bacteria degrade plant cell walls by secreting free, complementary enzymes that hydrolyze cellulose; however, some bacteria use large enzymatic assemblies called cellulosomes, which recruit complementary enzymes to protein scaffolds. The thermophilic bacterium Caldicellulosiruptor bescii uses an intermediate strategy, secreting many free cellulases that contain multiple catalytic domains. One of these, CelA, comprises a glycoside hydrolase family 9 and a family 48 catalytic domain, as well as three type III cellulose-binding modules. In the saccharification of a common cellulose standard, Avicel, CelA outperforms mixtures of commercially relevant exo- and endoglucanases. From transmission electron microscopy studies of cellulose after incubation with CelA, we report morphological features that suggest that CelA not only exploits the common surface ablation mechanism driven by general cellulase processivity, but also excavates extensive cavities into the surface of the substrate. These results suggest that nature's repertoire of cellulose digestion paradigms remain only partially discovered and understood. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=pbh&AN=93287317
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      – SubjectFull: Thermophilic bacteria
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