scholarly journals A Novel Carbohydrate-binding Protein Is a Component of the Plant Cell Wall-degrading Complex ofPiromyces equi

2001 ◽  
Vol 276 (46) ◽  
pp. 43010-43017 ◽  
Author(s):  
Alexander C. J. Freelove ◽  
David N. Bolam ◽  
Peter White ◽  
Geoffrey P. Hazlewood ◽  
Harry J. Gilbert
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Binding Protein ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Protein

scholarly journals Bacterial inducible expression of plant cell wall-binding protein YesO through conflict between Glycine max and saprophytic Bacillus subtilis

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Haruka Sugiura ◽  
Ayumi Nagase ◽  
Sayoko Oiki ◽  
Bunzo Mikami ◽  
Daisuke Watanabe ◽  
...  
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Glycine Max ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Binding Protein ◽  
Fermented Food ◽  
Physiological Status ◽  
Soybean Seeds ◽  
Initial Growth

Abstract Saprophytic bacteria and plants compete for limited nutrient sources. Bacillus subtilis grows well on steamed soybeans Glycine max to produce the fermented food, natto. Here we focus on bacterial responses in conflict between B. subtilis and G. max. B. subtilis cells maintained high growth rates specifically on non-germinating, dead soybean seeds. On the other hand, viable soybean seeds with germinating capability attenuated the initial growth of B. subtilis. Thus, B. subtilis cells may trigger saprophytic growth in response to the physiological status of G. max. Scanning electron microscope observation indicated that B. subtilis cells on steamed soybeans undergo morphological changes to form apertures, demonstrating cell remodeling during saprophytic growth. Further, transcriptomic analysis of B. subtilis revealed upregulation of the gene cluster, yesOPQR, in colonies growing on steamed soybeans. Recombinant YesO protein, a putative, solute-binding protein for the ATP-binding cassette transporter system, exhibited an affinity for pectin-derived oligosaccharide from plant cell wall. The crystal structure of YesO, in complex with the pectin oligosaccharide, was determined at 1.58 Å resolution. This study expands our knowledge of defensive and offensive strategies in interspecies competition, which may be promising targets for crop protection and fermented food production.

Analysis of the Structural and Functional Diversity of Plant Cell Wall Specific Family 6 Carbohydrate Binding Modules

Biochemistry ◽  
2009 ◽  
Vol 48 (43) ◽  
pp. 10395-10404 ◽  
Author(s):  
D. Wade Abbott ◽  
Elizabeth Ficko-Blean ◽  
Alicia Lammerts van Bueren ◽  
Artur Rogowski ◽  
Alan Cartmell ◽  
...  
Keyword(s):  
Cell Wall ◽  
Functional Diversity ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Modules

Glycoside hydrolase carbohydrate-binding modules as molecular probes for the analysis of plant cell wall polymers

2004 ◽  
Vol 326 (1) ◽  
pp. 49-54 ◽  
Author(s):  
Lesley McCartney ◽  
Harry J Gilbert ◽  
David N Bolam ◽  
Alisdair B Boraston ◽  
J.Paul Knox
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Glycoside Hydrolase ◽  
Plant Cell Wall ◽  
Molecular Probes ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Modules ◽  
Cell Wall Polymers

Characterization of a thermostable endoglucanase from Cellulomonas fimi ATCC484

2018 ◽  
Vol 96 (1) ◽  
pp. 68-76 ◽  
Author(s):  
Hirak Saxena ◽  
Bryan Hsu ◽  
Marc de Asis ◽  
Mirko Zierke ◽  
Lyann Sim ◽  
...  
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Hydrolytic Activity ◽  
Carbohydrate Binding ◽  
Cell Wall Polysaccharides ◽  
Cellulomonas Fimi ◽  
Thermal Denaturation Temperature ◽  
Mesophilic Bacterium

Bacteria in the genus Cellulomonas are well known as secretors of a variety of mesophilic carbohydrate degrading enzymes (e.g., cellulases and hemicellulases), active against plant cell wall polysaccharides. Recent proteomic analysis of the mesophilic bacterium Cellulomonas fimi ATCC484 revealed uncharacterized enzymes for the hydrolysis of plant cell wall biomass. Celf_1230 (CfCel6C), a secreted protein of Cellulomonas fimi ATCC484, is a novel member of the GH6 family of cellulases that could be successfully expressed in Escherichia coli. This enzyme displayed very little enzymatic/hydrolytic activity at 30 °C, but showed an optimal activity around 65 °C, and exhibited a thermal denaturation temperature of 74 °C. In addition, it also strongly bound to filter paper despite having no recognizable carbohydrate binding module. Our experiments show that CfCel6C is a thermostable endoglucanase with activity on a variety of β-glucans produced by an organism that struggles to grow above 30 °C.

scholarly journals Crystallization and preliminary crystallographic studies of a novel noncatalytic carbohydrate-binding module from theRuminococcus flavefacienscellulosome

2015 ◽  
Vol 71 (1) ◽  
pp. 45-48 ◽  
Author(s):  
Immacolata Venditto ◽  
Arun Goyal ◽  
Andrew Thompson ◽  
Luis M. A. Ferreira ◽  
Carlos M. G. A. Fontes ◽  
...  
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Catalytic Domain ◽  
Glycoside Hydrolase Family ◽  
Carbohydrate Binding ◽  
Cellulolytic Bacterium ◽  
Modular Architecture ◽  
Carbohydrate Binding Modules ◽  
Fundamental Biological Process

Microbial degradation of the plant cell wall is a fundamental biological process with considerable industrial importance. Hydrolysis of recalcitrant polysaccharides is orchestrated by a large repertoire of carbohydrate-active enzymes that display a modular architecture in which a catalytic domain is connectedvialinker sequences to one or more noncatalytic carbohydrate-binding modules (CBMs). CBMs direct the appended catalytic modules to their target substrates, thus potentiating catalysis. The genome of the most abundant ruminal cellulolytic bacterium,Ruminococcus flavefaciensstrain FD-1, provides an opportunity to discover novel cellulosomal proteins involved in plant cell-wall deconstruction. It encodes a modular protein comprising a glycoside hydrolase family 9 catalytic module (GH9) linked to two unclassified tandemly repeated CBMs (termed CBM-Rf6A and CBM-Rf6B) and a C-terminal dockerin. The novel CBM-Rf6A from this protein has been crystallized and data were processed for the native and a selenomethionine derivative to 1.75 and 1.5 Å resolution, respectively. The crystals belonged to orthorhombic and cubic space groups, respectively. The structure was solved by a single-wavelength anomalous dispersion experiment using theCCP4 program suite andSHELXC/D/E.

Mannan specific family 35 carbohydrate-binding module (CtCBM35) of Clostridium thermocellum: structure analysis and ligand binding

Biologia ◽  
2014 ◽  
Vol 69 (10) ◽  
Author(s):  
Arabinda Ghosh ◽  
Anil Verma ◽  
Ana Luis ◽  
Joana Bras ◽  
Carlos Fontes ◽  
...  
Keyword(s):  
Cell Wall ◽  
Ligand Binding ◽  
Binding Affinity ◽  
Plant Cell ◽  
Clostridium Thermocellum ◽  
Plant Cell Wall ◽  
Konjac Glucomannan ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Affinity Electrophoresis

AbstractThe three-dimensional model of the CtCBM35 (Cthe 2811), i.e. the family 35 carbohydrate binding module (CBM) from the Clostridium thermocellum family 26 glycoside hydrolase (GH) β-mannanase, generated by Modeller9v8 displayed predominance of β-sheets arranged as β-sandwich fold. Multiple sequence alignment of CtCBM35 with other CBM35s showed a conserved signature sequence motif Trp-Gly-Tyr, which is probably a specific determinant for mannan binding. Cloned CtCBM35 from Clostridium thermocellum ATCC 27405 was a homogenous, soluble 16 kDa protein. Ligand binding analysis of CtCBM35 by affinity electrophoresis displayed higher binding affinity against konjac glucomannan (K a = 2.5 × 105 M−1) than carob galactomannan (K a = 1.4 × 105 M−1). The presence of Ca2+ ions imparted slightly higher binding affinity of CtCBM35 against carob galactomannan and konjac glucomannan than without Ca2+ ion additive. However, CtCBM35 exhibited a low ligand-binding affinity K a = 2.5 × 10−5 M−1 with insoluble ivory nut mannan. Ligand binding study by fluorescence spectroscopy showed K a against konjac glucomannan and carob galactomannan, 2.4 × 105 M−1 and 1.44 × 105 M−1, and ΔG of binding −27.0 and −25.0 kJ/mol, respectively, substantiating the findings of affinity electrophoresis. Ca2+ ions escalated the thermostability of CtCBM35 and its melting temperature was shifted to 70°C from initial 55°C. Therefore thermostable CtCBM35 targets more β-(1,4)-manno-configured ligands from plant cell wall hemicellulosic reservoir. Thus a non-catalytic CtCBM35 of multienzyme cellulosomal enzymes may gain interest in the biofuel and food industry in the form of released sugars by targeting plant cell wall polysaccharides.

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