scholarly journals Presence of several cellulose-binding proteins in culture supernatant and cell lysate of Eubacterium cellulosolvens 5.

2001 ◽  
Vol 47 (6) ◽  
pp. 321-328 ◽  
Author(s):  
Atsushi Toyoda ◽  
Kazutoyo Yoda ◽  
Yutaka Nakamura ◽  
Hajime Minato
Keyword(s):  
Binding Proteins ◽  
Culture Supernatant ◽  
Cell Lysate ◽  
Eubacterium Cellulosolvens ◽  
Cellulose Binding

scholarly journals Purification of cellulose-binding proteins 1 and 2 from cell lysate of Fibrobacter succinogenes S85.

1993 ◽  
Vol 39 (4) ◽  
pp. 361-369 ◽  
Author(s):  
MAKOTO MITSUMORI ◽  
HAJIME MINATO
Keyword(s):  
Binding Proteins ◽  
Fibrobacter Succinogenes ◽  
Cell Lysate ◽  
Cellulose Binding

scholarly journals Presence of several cellulose-binding proteins in cell lysate of Fibrobacter succinogenes s85.

1993 ◽  
Vol 39 (3) ◽  
pp. 273-283 ◽  
Author(s):  
MAKOTO MITSUMORI ◽  
HAJIME MINATO
Keyword(s):  
Binding Proteins ◽  
Fibrobacter Succinogenes ◽  
Cell Lysate ◽  
Cellulose Binding

scholarly journals A possible role of cellulose-binding protein A (CBPA) in the adhesion of Eubacterium cellulosolvens 5 to cellulose

2003 ◽  
Vol 49 (4) ◽  
pp. 245-250 ◽  
Author(s):  
Atsushi Toyoda ◽  
Kazunori Takano ◽  
Hajime Minato
Keyword(s):  
Binding Protein ◽  
Protein A ◽  
Eubacterium Cellulosolvens ◽  
Cellulose Binding

scholarly journals Steered molecular dynamics simulations reveal the role of Ca2+ in regulating mechanostability of cellulose-binding proteins

2018 ◽  
Vol 20 (35) ◽  
pp. 22674-22680 ◽  
Author(s):  
Melissabye Gunnoo ◽  
Pierre-André Cazade ◽  
Adam Orlowski ◽  
Mateusz Chwastyk ◽  
Haipei Liu ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Binding Proteins ◽  
Mechanical Stability ◽  
Binding Specificity ◽  
Steered Molecular Dynamics ◽  
Dynamics Simulations ◽  
Cellulose Binding ◽  
High Mechanical Stability

Cellulosome nanomachines utilise binding specificity and high mechanical stability in breaking down cellulose.

scholarly journals Distribution of cellulose-binding proteins among the representative strainsof rumen bacteria.

1995 ◽  
Vol 41 (4) ◽  
pp. 297-306 ◽  
Author(s):  
MAKOTO MITSUMORI ◽  
HAJIME MINATO
Keyword(s):  
Binding Proteins ◽  
Rumen Bacteria ◽  
Cellulose Binding

Unique calcium-dependent hydrophobic binding proteins: possible independent mediators of intracellular calcium distinct from calmodulin

1984 ◽  
Vol 72 (1) ◽  
pp. 121-133
Author(s):  
P.B. Moore ◽  
N. Kraus-Friedmann ◽  
J.R. Dedman
Keyword(s):  
Calcium Binding ◽  
Binding Proteins ◽  
Deae Cellulose ◽  
Heat Stability ◽  
Binding Characteristics ◽  
Calcium Dependent ◽  
Cellular Processes ◽  
Hydrophobic Site ◽  
Hydrophobic Binding ◽  
Cellulose Binding

Calcium-dependent regulation of cellular processes is mediated by specific intracellular proteins. A newly described set of proteins isolated from chicken gizzard with Mr of 67 X 10(3), 35 X 10(3), 33 X 10(3) and 30 X 10(3) also express a hydrophobic site in the presence of calcium. These proteins are isolated from several other cellular tissues and are termed calcimedins. These proteins differ from calmodulin in isoelectric point, DEAE-cellulose binding characteristics and heat stability. The calcimedins do not activate calmodulin-dependent cyclic nucleotide phosphodiesterase but do activate a hepatic microsomal Ca2+ -ATPase system. Hence, the possibility is opened that calcium regulation of cellular processes is mediated by calcium-binding proteins in addition to calmodulin.

scholarly journals Comparative Biochemical and Structural Analysis of Novel Cellulose Binding Proteins (Tāpirins) from Extremely Thermophilic Caldicellulosiruptor Species

2018 ◽  
Vol 85 (3) ◽  
Author(s):  
Laura L. Lee ◽  
William S. Hart ◽  
Vladimir V. Lunin ◽  
Markus Alahuhta ◽  
Yannick J. Bomble ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Microcrystalline Cellulose ◽  
Binding Proteins ◽  
Amino Acid Sequence Identity ◽  
Plant Biomass ◽  
Three Dimensional ◽  
Content Type ◽  
Sequence Identity ◽  
Cellulose Binding

ABSTRACT Genomes of extremely thermophilic Caldicellulosiruptor species encode novel cellulose binding proteins, called tāpirins, located proximate to the type IV pilus locus. The C-terminal domain of Caldicellulosiruptor kronotskyensis tāpirin 0844 (Calkro_0844) is structurally unique and has a cellulose binding affinity akin to that seen with family 3 carbohydrate binding modules (CBM3s). Here, full-length and C-terminal versions of tāpirins from Caldicellulosiruptor bescii (Athe_1870), Caldicellulosiruptor hydrothermalis (Calhy_0908), Caldicellulosiruptor kristjanssonii (Calkr_0826), and Caldicellulosiruptor naganoensis (NA10_0869) were produced recombinantly in Escherichia coli and compared to Calkro_0844. All five tāpirins bound to microcrystalline cellulose, switchgrass, poplar, and filter paper but not to xylan. Densitometry analysis of bound protein fractions visualized by SDS-PAGE revealed that Calhy_0908 and Calkr_0826 (from weakly cellulolytic species) associated with the cellulose substrates to a greater extent than Athe_1870, Calkro_0844, and NA10_0869 (from strongly cellulolytic species). Perhaps this relates to their specific needs to capture glucans released from lignocellulose by cellulases produced in Caldicellulosiruptor communities. Calkro_0844 and NA10_0869 share a higher degree of amino acid sequence identity (>80% identity) with each other than either does with Athe_1870 (∼50%). The levels of amino acid sequence identity of Calhy_0908 and Calkr_0826 to Calkro_0844 were only 16% and 36%, respectively, although the three-dimensional structures of their C-terminal binding regions were closely related. Unlike the parent strain, C. bescii mutants lacking the tāpirin genes did not bind to cellulose following short-term incubation, suggesting a role in cell association with plant biomass. Given the scarcity of carbohydrates in neutral terrestrial hot springs, tāpirins likely help scavenge carbohydrates from lignocellulose to support growth and survival of Caldicellulosiruptor species. IMPORTANCE The mechanisms by which microorganisms attach to and degrade lignocellulose are important to understand if effective approaches for conversion of plant biomass into fuels and chemicals are to be developed. Caldicellulosiruptor species grow on carbohydrates from lignocellulose at elevated temperatures and have biotechnological significance for that reason. Novel cellulose binding proteins, called tāpirins, are involved in the way that Caldicellulosiruptor species interact with microcrystalline cellulose, and additional information about the diversity of these proteins across the genus, including binding affinity and three-dimensional structural comparisons, is provided here.

Detection of cellulose-binding proteins in electrophoresis gels by filter paper affinity blotting

1988 ◽  
Vol 174 (1) ◽  
pp. 204-208 ◽  
Author(s):  
Larry Montgomery ◽  
Yung-Kang Fu
Keyword(s):  
Filter Paper ◽  
Binding Proteins ◽  
Cellulose Binding

scholarly journals In Silico Characterization of Meloidogyne Genus Nematode Cellulose Binding Proteins

2019 ◽  
Vol 62 ◽  
Author(s):  
Alana Manoela Fraga Menezes ◽  
Edilton de Albuquerque Cavalcanti Junior ◽  
Luiza Suely Semen Martins ◽  
Rômulo Maciel de Moraes Filho
Keyword(s):  
In Silico ◽  
Binding Proteins ◽  
In Silico Characterization ◽  
Cellulose Binding

Labeling and Purification of Cellulose-Binding Proteins for High Resolution Fluorescence Applications

2009 ◽  
Vol 81 (19) ◽  
pp. 7981-7987 ◽  
Author(s):  
Jose M. Moran-Mirabal ◽  
Stephane C. Corgie ◽  
Jacob C. Bolewski ◽  
Hanna M. Smith ◽  
Benjamin R. Cipriany ◽  
...  
Keyword(s):  
High Resolution ◽  
Binding Proteins ◽  
Cellulose Binding
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