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In vitro and in vivo characterization of three Cellvibrio japonicus glycoside hydrolase family 5 members reveals potent xyloglucan backbone-cleaving functions

Overview of attention for article published in Biotechnology for Biofuels and Bioproducts, February 2018
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Title
In vitro and in vivo characterization of three Cellvibrio japonicus glycoside hydrolase family 5 members reveals potent xyloglucan backbone-cleaving functions
Published in
Biotechnology for Biofuels and Bioproducts, February 2018
DOI 10.1186/s13068-018-1039-6
Pubmed ID
Authors

Mohamed A. Attia, Cassandra E. Nelson, Wendy A. Offen, Namrata Jain, Gideon J. Davies, Jeffrey G. Gardner, Harry Brumer

Abstract

Xyloglucan (XyG) is a ubiquitous and fundamental polysaccharide of plant cell walls. Due to its structural complexity, XyG requires a combination of backbone-cleaving and sidechain-debranching enzymes for complete deconstruction into its component monosaccharides. The soil saprophyteCellvibrio japonicushas emerged as a genetically tractable model system to study biomass saccharification, in part due to its innate capacity to utilize a wide range of plant polysaccharides for growth. Whereas the downstream debranching enzymes of the xyloglucan utilization system ofC. japonicushave been functionally characterized, the requisite backbone-cleavingendo-xyloglucanases were unresolved. Combined bioinformatic and transcriptomic analyses implicated three glycoside hydrolase family 5 subfamily 4 (GH5_4) members, with distinct modular organization, as potential keystoneendo-xyloglucanases inC. japonicus. Detailed biochemical and enzymatic characterization of the GH5_4 modules of all three recombinant proteins confirmed particularly high specificities for the XyG polysaccharide versus a panel of other cell wall glycans, including mixed-linkage beta-glucan and cellulose. Moreover, product analysis demonstrated that all three enzymes generated XyG oligosaccharides required for subsequent saccharification by knownexo-glycosidases. Crystallographic analysis of GH5D, which was the only GH5_4 member specifically and highly upregulated during growth on XyG, in free, product-complex, and active-site affinity-labelled forms revealed the molecular basis for the exquisite XyG specificity among these GH5_4 enzymes. Strikingly, exhaustive reverse-genetic analysis of all three GH5_4 members and a previously biochemically characterized GH74 member failed to reveal a growth defect, thereby indicating functional compensation in vivo, both among members of this cohort and by other, yet unidentified, xyloglucanases inC. japonicus. Our systems-based analysis indicates distinct substrate-sensing (GH74, GH5E, GH5F) and attack-mounting (GH5D) functions for theendo-xyloglucanases characterized here. Through a multi-faceted, molecular systems-based approach, this study provides a new insight into the saccharification pathway of xyloglucan utilization system ofC. japonicus. The detailed structural-functional characterization of three distinct GH5_4endo-xyloglucanases will inform future bioinformatic predictions across species, and provides new CAZymes with defined specificity that may be harnessed in industrial and other biotechnological applications.

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The data shown below were collected from the profiles of 4 X users who shared this research output. Click here to find out more about how the information was compiled.
Mendeley readers

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The data shown below were compiled from readership statistics for 48 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 48 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 12 25%
Student > Bachelor 8 17%
Student > Master 8 17%
Researcher 6 13%
Student > Doctoral Student 4 8%
Other 2 4%
Unknown 8 17%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 16 33%
Agricultural and Biological Sciences 7 15%
Engineering 5 10%
Chemistry 4 8%
Pharmacology, Toxicology and Pharmaceutical Science 2 4%
Other 4 8%
Unknown 10 21%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 2. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 22 March 2018.
All research outputs
#16,053,755
of 25,382,440 outputs
Outputs from Biotechnology for Biofuels and Bioproducts
#882
of 1,578 outputs
Outputs of similar age
#199,018
of 344,026 outputs
Outputs of similar age from Biotechnology for Biofuels and Bioproducts
#26
of 49 outputs
Altmetric has tracked 25,382,440 research outputs across all sources so far. This one is in the 34th percentile – i.e., 34% of other outputs scored the same or lower than it.
So far Altmetric has tracked 1,578 research outputs from this source. They receive a mean Attention Score of 4.9. This one is in the 40th percentile – i.e., 40% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 344,026 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 39th percentile – i.e., 39% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 49 others from the same source and published within six weeks on either side of this one. This one is in the 40th percentile – i.e., 40% of its contemporaries scored the same or lower than it.