Frontiers in Microbiology, 2017 The rumen bacterium Cellulosilyticum ruminicola H1 efficiently hydrolyzes cellulose. To gain insights into the regulatory mechanisms of cellulase synthesis, comparative transcriptome analysis was conducted for cultures grown on 2% filter paper, 0.5 and 0.
Shanzhen Li +7 more
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Designer Glycolysomes: Colocalisation of Glycolytic Enzymes on a Cellulosome-Based Synthetic Protein Scaffold. [PDF]
Microb BiotechnolThe first three Escherichia coli glycolytic enzymes were converted to the docking enzyme mode and subsequently scaffolded. Increasing copies of the rate‐limiting enzyme boosted the overall performance. At lower enzyme densities, the proximity effects provided by scaffold‐colocalisation result in a higher product yield compared to free docking enzymes ...
Elias M +4 more
europepmc +2 more sources
The Trichohyalin-Like Protein Scaffoldin Is Expressed in the Multilayered Periderm during Development of Avian Beak and Egg Tooth. [PDF]
Genes (Basel), 2021 Scaffoldin, an S100 fused-type protein (SFTP) with high amino acid sequence similarity to the mammalian hair follicle protein trichohyalin, has been identified in reptiles and birds, but its functions are not yet fully understood. Here, we investigated the expression pattern of scaffoldin and cornulin, a related SFTP, in the developing beaks of birds ...
Mlitz V +4 more
europepmc +4 more sources
Structure of CBM3b of the major cellulosomal scaffoldin subunit ScaA fromAcetivibrio cellulolyticus [PDF]
Acta Crystallographica Section F Structural Biology and Crystallization Communications, 2011 The carbohydrate-binding module (CBM) of the major scaffoldin subunit ScaA of the cellulosome of Acetivibrio cellulolyticus is classified as a family 3b CBM and binds strongly to cellulose. The CBM3b was overexpressed, purified and crystallized, and its three-dimensional structure was determined. The structure contained a nickel-binding site located at
Oren, Yaniv +5 more
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Scaffoldin Modules Serving as “Cargo” Domains To Promote the Secretion of Heterologous Cellulosomal Cellulases by Clostridium acetobutylicum [PDF]
Applied and Environmental Microbiology, 2011 ABSTRACT The secretion of large heterologous cellulases by Clostridium acetobutylicum was formerly shown to be deleterious. To circumvent this issue, various scaffoldins' modules were grafted at their N termini.
Angélique, Chanal +4 more
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mBio, 2018 Cellulosomes are multienzyme complexes produced by anaerobic, cellulolytic bacteria for highly efficient breakdown of plant cell wall polysaccharides.
Lior Artzi +6 more
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A Novel Cellulosomal Scaffoldin from Acetivibrio cellulolyticus That Contains a Family 9 Glycosyl Hydrolase [PDF]
Journal of Bacteriology, 1999 ABSTRACT A novel cellulosomal scaffoldin gene, termed cipV , was identified and sequenced from the mesophilic cellulolytic anaerobe Acetivibrio cellulolyticus . Initial identification of the protein was based on a combination of properties, including its high molecular weight ...
S Y, Ding +4 more
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Scientific Reports, 2017 Abtract Cellulosomes are sophisticated multi-enzymatic nanomachines produced by anaerobes to effectively deconstruct plant structural carbohydrates.
Pedro Bule +9 more
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Expression, purification, and characterization of the cellulose-binding domain of the scaffoldin subunit from the cellulosome of Clostridium thermocellum [PDF]
Applied and Environmental Microbiology, 1995 The major cellulose-binding domain (CBD) from the cellulosome of Clostridium thermocellum YS was cloned and overexpressed in Escherichia coli. The expressed protein was purified efficiently by a modification of a novel procedure termed affinity digestion.
E, Morag +6 more
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Cell‐surface exposure of a hybrid 3‐cohesin scaffoldin allowing the functionalization of Escherichia coli envelope [PDF]
Biotechnology and Bioengineering, 2020 AbstractCellulosomes are large plant cell wall degrading complexes secreted by some anaerobic bacteria. They are typically composed of a major scaffolding protein containing multiple receptors called cohesins, which tightly anchor a small complementary module termed dockerin harbored by the cellulosomal enzymes.
Nicolas Vita +2 more
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