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

scholarly journals The three dimensional structure of Bovine Salivary Protein 30b (BSP30b) and its interaction with specific rumen bacteria

2018 ◽  
Author(s):  
Heng Zhang ◽  
Judith Burrows ◽  
Graeme L. Card ◽  
Graeme Attwood ◽  
Thomas T. Wheeler ◽  
...  
Keyword(s):  
Oleic Acid ◽  
Binding Proteins ◽  
Bacterial Species ◽  
Fluorescent Microscopy ◽  
Salivary Protein ◽  
Lipid Binding ◽  
Dimensional Structure ◽  
Rumen Bacteria ◽  
Abundant Protein

AbstractBovine Salivary Protein 30b (BSP30b) is a member of the tubular lipid-binding (TULIP) superfamily that includes the human bactericidal/permeability-increasing proteins (BPI), lipopolysaccharide binding proteins (LBP) and palate, lung, and nasal epithelium carcinoma-21 associated proteins (PLUNC). BSP30b is most closely related to the PLUNC family and is predominantly found in bovine saliva. There are four BSP30 isoforms (BSP30a-d) and collectively, they are the most abundant protein component of bovine saliva. The PLUNC family members are proposed to be lipid binding proteins, although in most cases their lipid ligands are unknown. Here, we present the X-ray crystal structure of BSP30b at 2.0 Å resolution. We used a double methionine mutant and Se-Met SAD phasing to solve the structure. The structure adopts a curved cylindrical form with a hydrophobic channel formed by an α/β wrap, which is consistent with the TULIP superfamily. The structure of BSP30b in complex with oleic acid is also presented where the ligand is accommodated within the hydrophobic channel. The electron density for oleic acid suggests that the ligand is only partially occupied in the binding site implying that oleic acid may not be the preferred ligand. GFP-tagged BSP30b binds to the surface of olive oil droplets, as observed under fluorescent microscopy, and acts as a surfactant consistent with its association with decreased susceptibility to bloat in cattle. Bacteria extracted directly from bovine rumen contents indicate that the GFP_BSP30b fusion protein binds to a small number of selected bacterial species in vivo. These results suggest that BSP30b may bind to bacterial lipids from specific species and that this abundant protein may have important biological roles via interacting with rumen bacteria during feeding and rumination.

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.

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.

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

scholarly journals Outer Membrane Proteins of Fibrobacter succinogenes with Potential Roles in Adhesion to Cellulose and in Cellulose Digestion

2007 ◽  
Vol 189 (19) ◽  
pp. 6806-6815 ◽  
Author(s):  
Hyun-Sik Jun ◽  
Meng Qi ◽  
Joshua Gong ◽  
Emmanuel E. Egbosimba ◽  
Cecil W. Forsberg
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Binding Proteins ◽  
Outer Membrane Proteins ◽  
Mass Spectrometry Analysis ◽  
Crystalline Cellulose ◽  
Fibrobacter Succinogenes ◽  
Essential Components ◽  
Mutant Strains ◽  
Cellulose Binding

ABSTRACT Comparative analysis of binding of intact glucose-grown Fibrobacter succinogenes strain S85 cells and adhesion-defective mutants AD1 and AD4 to crystalline and acid-swollen (amorphous) cellulose showed that strain S85 bound efficiently to both forms of cellulose while mutant Ad1 bound to acid-swollen cellulose, but not to crystalline cellulose, and mutant Ad4 did not bind to either. One- and two-dimensional electrophoresis (2-DE) of outer membrane cellulose binding proteins and of outer membranes, respectively, of strain S85 and adhesion-defective mutant strains in conjunction with mass spectrometry analysis of tryptic peptides was used to identify proteins with roles in adhesion to and digestion of cellulose. Examination of the binding to cellulose of detergent-solubilized outer membrane proteins from S85 and mutant strains revealed six proteins in S85 that bound to crystalline cellulose that were absent from the mutants and five proteins in Ad1 that bound to acid-swollen cellulose that were absent from Ad4. Twenty-five proteins from the outer membrane fraction of cellulose-grown F. succinogenes were identified by 2-DE, and 16 of these were up-regulated by growth on cellulose compared to results with growth on glucose. A protein identified as a Cl-stimulated cellobiosidase was repressed in S85 cells growing on glucose and further repressed in the mutants, while a cellulose-binding protein identified as pilin was unchanged in S85 grown on glucose but was not produced by the mutants. The candidate differential cellulose binding proteins of S85 and the mutants and the proteins induced by growth of S85 on cellulose provide the basis for dissecting essential components of the cellulase system of F. succinogenes.

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