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3D Genome Engineering: Current Advances and Therapeutic Opportunities in Human Diseases. [PDF]

Research (Wash D C)
Jiang X, Wang X, Shen S, Hou S, Yu C.
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Resonance assignments of a cellulosomal double-dockerin from Clostridium thermocellum

Biomolecular NMR Assignments, 2018
Cellulosomes are highly efficient multienzyme complexes for lignocellulose degradation secreted by some lignocellulolytic bacteria. Cellulosomes are assembled through protein modules named cohesin and dockerin, and multiple cohesin modules in the scaffold protein generally determine the complexity of the cellulosomes. Some cellulosomal proteins contain
Chao Chen, Hongwu Yang, Jinsong Xuan, Q. Cui, Yingang Feng   +4 more
semanticscholar   +3 more sources

Single versus dual-binding conformations in cellulosomal cohesin-dockerin complexes.

Current Opinion in Structural Biology, 2016
Cohesins and dockerins are complementary interacting protein modules that form stable and highly specific receptor-ligand complexes. They play a crucial role in the assembly of cellulose-degrading multi-enzyme complexes called cellulosomes and have potential applicability in several technology areas, including biomass conversion processes.
M. Nash, Steven P. Smith, C. Fontes, E. Bayer   +3 more
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Dual binding mode in cohesin-dockerin complexes as assessed through stretching studies.

The Journal of Chemical Physics, 2016
A recent experimental study by Jobst et al. of stretching of a wild-type (WT) cohesin-dockerin complex has identified two kinds of the force-displacement patterns, with a single or double-peaked final rupture, which are termed “short” and “long” here. This duality has been interpreted as arising from the existence of two kinds of binding.
M. Wojciechowski, M. Cieplak
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Species-specificity of the cohesin-dockerin interaction betweenClostridium thermocellum andClostridium cellulolyticum: Prediction of specificity determinants of the dockerin domain

Proteins: Structure, Function, and Genetics, 1997
The cross-species specificity of the cohesin-dockerin interaction, which defines the incorporation of the enzymatic subunits into the cellulosome complex, has been investigated. Cohesin-containing segments from the cellulosomes of two different species, Clostridium thermocellum and Clostridium cellulolyticum, were allowed to interact with cellulosomal (
S, Pagès, A, Bélaïch, J P, Bélaïch, E, Morag, R, Lamed, Y, Shoham, E A, Bayer   +6 more
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Cohesin-dockerin recognition in cellulosome assembly: Experiment versus hypothesis

Proteins: Structure, Function, and Genetics, 2000
The cohesin-dockerin interaction provides the basis for incorporation of the individual enzymatic subunits into the cellulosome complex. In a previous article (Pagés et al., Proteins 1997;29:517-527) we predicted that four amino acid residues of the approximately 70-residue dockerin domain would serve as recognition codes for binding to the cohesin ...
A, Mechaly, S, Yaron, R, Lamed, H P, Fierobe, A, Belaich, J P, Belaich, Y, Shoham, E A, Bayer   +7 more
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Cohesin-Dockerin Interactions and Folding

2014
Many investigations were conducted to characterize the cohesin-dockerin interactions. These studies include measuring cohesin-dockerin affinity, identifying critical amino acid residues by site-directed mutagenesis, and determining the molecular structures of the dockerin, cohesin, and its complex.
J. H. David Wu, Michael Newcomb, Kazuo Sakka   +2 more
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Resonance assignments of cohesin and dockerin domains from Clostridium acetobutylicum ATCC824

Biomolecular NMR Assignments, 2012
Cohesin and dockerin domains are critical assembling components of cellulosome, a large extracellular multienzyme complex which is used by anaerobic cellulolytic bacteria to efficiently degrade lignocellulose. According to sequence homology, cohesins can be divided into three major groups, whereas cohesins from Clostridium acetobutylicum are beyond ...
Zhenling, Cui, Yifei, Li, Yan, Xiao, Yingang, Feng, Qiu, Cui, Qui, Cui   +5 more
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Cellulosome from Clostridium cellulolyticum: Molecular Study of the Dockerin/Cohesin Interaction

Biochemistry, 1999
Clostridium cellulolyticum produces cellulolytic complexes (cellulosomes) made of 10-13 cell wall degrading enzymes tightly bound to a scaffolding protein (CipC) by means of their dockerin domain. It has previously been shown that the receptor domains in CipC are the cohesin domains and that the cohesin/dockerin interaction is calcium-dependent. In the
H P, Fierobe, S, Pagès, A, Bélaïch, S, Champ, D, Lexa, J P, Bélaïch   +5 more
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Cohesin‐dockerin microarray: Diverse specificities between two complementary families of interacting protein modules

PROTEOMICS, 2008
AbstractThe cellulosome is an intricate multienzyme complex, designed for efficient degradation of plant cell wall polysaccharides, notably cellulose. The supramolecular cellulosome architecture in different bacteria is the consequence of the types and specificities of the interacting cohesin and dockerin modules, borne by the different cellulosomal ...
Rachel, Haimovitz, Yoav, Barak, Ely, Morag, Milana, Voronov-Goldman, Yuval, Shoham, Raphael, Lamed, Edward A, Bayer   +6 more
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