Cohesin-Dockerin Interaction in Cellulosome Assembly [PDF]
The assembly of enzyme components into the cellulosome complex is dictated by the cohesin-dockerin interaction. In a recent article (Mechaly, A., Yaron, S., Lamed, R., Fierobe, H.-P., Belaich, A., Belaich, J.-P., Shoham, Y., and Bayer, E. A. (2000) Proteins 39, 170-177), we provided experimental evidence that four previously predicted dockerin residues
Adva Mechaly +6 more
openaire +4 more sources
Affinity-induced covalent protein-protein ligation via the SpyCatcher-SpyTag interaction
Production of economically viable bioethanol is potentially an environmentally and financially worthwhile endeavor. One major source for fermentable sugars is lignocellulose. However, lignocellulosic biomass is difficult to degrade, owing to its inherent
Jacob O. Fierer +6 more
doaj +1 more source
Designing chimeric enzymes inspired by fungal cellulosomes
Cellulosomes are synthesized by anaerobic bacteria and fungi to degrade lignocellulose via synergistic action of multiple enzymes fused to a protein scaffold.
Sean P. Gilmore +4 more
doaj +1 more source
Effects of dockerin domains onNeocallimastix frontalisxylanases [PDF]
Two xylanase genes were cloned from the anaerobic fungus Neocallimastix frontalis. Xyn11A had a modular structure of two catalytic domains and two dockerin domains, while Xyn11B had one catalytic domain and two dockerin domains. The characteristics of the xylanases with and without dockerin domains were investigated.
Ya-Hui, Huang +2 more
openaire +2 more sources
Noncellulosomal cohesin- and dockerin-like modules in the three domains of life [PDF]
The high-affinity cohesin-dockerin interaction was originally discovered as modular components, which mediate the assembly of the various subunits of the multienzyme cellulosome complex that characterizes some cellulolytic bacteria. Until recently, the presence of cohesins and dockerins within a bacterial proteome was considered a definitive signature ...
Ayelet, Peer +4 more
openaire +2 more sources
Cellulosomics, a gene-centric approach to investigating the intraspecific diversity and adaptation of Ruminococcus flavefaciens within the rumen. [PDF]
BackgroundThe bovine rumen maintains a diverse microbial community that serves to break down indigestible plant substrates. However, those bacteria specifically adapted to degrade cellulose, the major structural component of plant biomass, represent a ...
Jennifer M Brulc +13 more
doaj +1 more source
Cohesin-dockerin interactions within and between Clostridium josui and Clostridium thermocellum: binding selectivity between cognate dockerin and cohesin domains and species specificity. [PDF]
The cellulosome components are assembled into the cellulosome complex by the interaction between one of the repeated cohesin domains of a scaffolding protein and the dockerin domain of an enzyme component. We prepared five recombinant cohesin polypeptides of the Clostridium thermocellum scaffolding protein CipA, two dockerin polypeptides of C ...
Sadanari, Jindou +9 more
openaire +2 more sources
Anaerobic fungi and methanogenic archaea are two classes of microorganisms found in the rumen microbiome that metabolically interact during lignocellulose breakdown.
Jennifer L. Brown +15 more
doaj +1 more source
Presenting a focused review on novel methods for protein engineering, this article delves into cutting‐edge advancements in the field of yeast surface display. Central themes include titratable avidity, on‐yeast serology, unconventional antigens including cell lysates and membrane proteins, expanded chemistry, noncanonical amino acids, and continuous ...
Joanan Lopez-Morales +8 more
wiley +1 more source
Cohesin-Dockerin Interactions of Cellulosomal Subunits of Clostridium cellulovorans [PDF]
ABSTRACT The cellulosome of Clostridium cellulovorans consists of three major subunits: CbpA, EngE, and ExgS. The C. cellulovorans scaffolding protein (CbpA) contains nine hydrophobic repeated domains (cohesins) for the binding of enzymatic subunits.
J S, Park, Y, Matano, R H, Doi
openaire +2 more sources

