Evidence map›Paper›PMID 26814128›Full record

ArticleThe Journal of biological chemistry2016

Multidomain, Surface Layer-associated Glycoside Hydrolases Contribute to Plant Polysaccharide Degradation by Caldicellulosiruptor Species.

Jonathan M Conway, William S Pierce, Jaycee H Le, George W Harper, John H Wright, Allyson L Tucker, Jeffrey V Zurawski, Laura L Lee, Sara E Blumer-Schuette, Robert M Kelly

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
7.8field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

33 citing papers in PubMed, 57 citations in OpenAlex.

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  14. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 1 institution in 1 country.

Jonathan M ConwayFrom the Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, North Carolina 27695.
William S PierceFrom the Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, North Carolina 27695.
Jaycee H LeFrom the Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, North Carolina 27695.
George W HarperFrom the Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, North Carolina 27695.
John H WrightFrom the Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, North Carolina 27695.
Allyson L TuckerFrom the Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, North Carolina 27695.
Jeffrey V ZurawskiFrom the Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, North Carolina 27695.
Laura L LeeFrom the Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, North Carolina 27695.
Sara E Blumer-SchuetteFrom the Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, North Carolina 27695.
Robert M KellyFrom the Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, North Carolina 27695 rmkelly@ncsu.edu.
North Carolina State University · US

Funding

Molecular Biotechnology Training at North Carolina State UniversityT32GM008776 · NIGMS · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI KELLY, ROBERT M · 2000 to 2019
$3.9M
NIGMS NIH HHS T32 GM008776-11
6 · The paper itself

Abstract

The genome of the extremely thermophilic bacterium Caldicellulosiruptor kronotskyensisencodes 19 surface layer (S-layer) homology (SLH) domain-containing proteins, the most in any Caldicellulosiruptorspecies genome sequenced to date. These SLH proteins include five glycoside hydrolases (GHs) and one polysaccharide lyase, the genes for which were transcribed at high levels during growth on plant biomass. The largest GH identified so far in this genus, Calkro_0111 (2,435 amino acids), is completely unique toC. kronotskyensisand contains SLH domains. Calkro_0111 was produced recombinantly inEscherichia colias two pieces, containing the GH16 and GH55 domains, respectively, as well as putative binding and spacer domains. These displayed endo- and exoglucanase activity on the β-1,3-1,6-glucan laminarin. A series of additional truncation mutants of Calkro_0111 revealed the essential architectural features required for catalytic function. Calkro_0402, another of the SLH domain GHs inC. kronotskyensis, when produced inE. coli, was active on a variety of xylans and β-glucans. Unlike Calkro_0111, Calkro_0402 is highly conserved in the genus Caldicellulosiruptorand among other biomass-degrading Firmicutes but missing from Caldicellulosiruptor bescii As such, the gene encoding Calkro_0402 was inserted into the C. besciigenome, creating a mutant strain with its S-layer extensively decorated with Calkro_0402. This strain consequently degraded xylans more extensively than wild-typeC. bescii The results here provide new insights into the architecture and role of SLH domain GHs and demonstrate that hemicellulose degradation can be enhanced through non-native SLH domain GHs engineered into the genomes of Caldicellulosiruptorspecies.

Indexed as

Genome, BacterialBacterial ProteinsCloning, MolecularEscherichia coliEubacterialesGene ExpressionGlucansGlycoside HydrolasesKineticsMutationPhylogenyPolysaccharidesProtein BindingProtein EngineeringProtein Structure, TertiaryRecombinant ProteinsBacterial ProteinsGlucansGlycoside HydrolaseshemicelluloselaminaranPolysaccharidesRecombinant ProteinsXylansbiofuelCaldicellulosiruptorcell surfacecell surface enzymeenzymeglycoside hydrolaselignocelluloseplant cell wallS-layer

Identifiers

PMID26814128
PMCPMC4807261
OpenAlexW2280423063

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.