Standalone cohesin as a molecular shuttle in cellulosome assembly

Voronov-Goldman, Milana; Yaniv, Oren; Gül, Özgür; Yoffe, Hagar; Salama-Alber, Orly; Slutzki, Michal; Levy-Assaraf, Maly; Jindou, Sadanari; Shimon, Linda J. W.; Borovok, Ilya; Bayer, Edward A.; Lamed, Raphael; Frolow, Felix

doi:10.1016/j.febslet.2015.04.013

Cited by 14 publications

(11 citation statements)

References 41 publications

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“…However, it has also been observed that certain dockerins that lack structural symmetry display a single‐binding mode (Bras et al ., ). In those dockerin sequences, each segment represents separate binding interfaces that can recognize a different cohesin (Pinheiro et al ., ; Voronov‐Goldman et al ., ). The latter characteristics of known dockerin sequences reflect the complexity and diversity in cohesin–dockerin interactions that contribute to dockerin flexibility in case of steric interferences and improved response to the dynamic process of plant cell wall degradation (Carvalho et al ., ).…”

Section: Resultsmentioning

confidence: 97%

Enzymatic profiling of cellulosomal enzymes from the human gut bacterium, Ruminococcus champanellensis, reveals a fine‐tuned system for cohesin‐dockerin recognition

Moraïs

David

Bensoussan

et al. 2015

Environmental Microbiology

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Ruminococcus champanellensis is considered a keystone species in the human gut that degrades microcrystalline cellulose efficiently and contains the genetic elements necessary for cellulosome production. The basic elements of its cellulosome architecture, mainly cohesin and dockerin modules from scaffoldins and enzyme-borne dockerins, have been characterized recently. In this study, we cloned, expressed and characterized all of the glycoside hydrolases that contain a dockerin module. Among the 25 enzymes, 10 cellulases, 4 xylanases, 3 mannanases, 2 xyloglucanases, 2 arabinofuranosidases, 2 arabinanases and one β-glucanase were assessed for their comparative enzymatic activity on their respective substrates. The dockerin specificities of the enzymes were examined by ELISA, and 80 positives out of 525 possible interactions were detected. Our analysis reveals a fine-tuned system for cohesin-dockerin specificity and the importance of diversity among the cohesin-dockerin sequences. Our results imply that cohesin-dockerin pairs are not necessarily assembled at random among the same specificity types, as generally believed for other cellulosome-producing bacteria, but reveal a more organized cellulosome architecture. Moreover, our results highlight the importance of the cellulosome paradigm for cellulose and hemicellulose degradation by R. champanellensis in the human gut.

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Section: Resultsmentioning

confidence: 97%

Enzymatic profiling of cellulosomal enzymes from the human gut bacterium, Ruminococcus champanellensis, reveals a fine‐tuned system for cohesin‐dockerin recognition

Moraïs

David

Bensoussan

et al. 2015

Environmental Microbiology

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“…The additional cell-free scaffoldins, ScaM1 and ScaM2, contain type II cohesins along with a CBM3 module that would target the attached enzymes to the substrate. In contrast, monovalent (single cohesin) free scaffoldins (ScaW1, ScaW2) may either serve as molecular shuttles, stabilize enzyme activity through cohesin–dockerin interaction, or serve a regulatory function [ 63 – 65 ]. Multiple monovalent scaffoldins are widespread among complex cellulosome-producing bacteria [ 16 , 19 , 66 ] and could be part of a regulatory mechanism for cellulosomal composition.…”

Section: Discussionmentioning

confidence: 99%

Unique organization and unprecedented diversity of the Bacteroides (Pseudobacteroides) cellulosolvens cellulosome system

Zhivin

Dassa

Moraïs

et al. 2017

Biotechnol Biofuels

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Background (Pseudo) Bacteroides cellulosolvens is an anaerobic, mesophilic, cellulolytic, cellulosome-producing clostridial bacterium capable of utilizing cellulose and cellobiose as carbon sources. Recently, we sequenced the B. cellulosolvens genome, and subsequent comprehensive bioinformatic analysis, herein reported, revealed an unprecedented number of cellulosome-related components, including 78 cohesin modules scattered among 31 scaffoldins and more than 200 dockerin-bearing ORFs. In terms of numbers, the B. cellulosolvens cellulosome system represents the most intricate, compositionally diverse cellulosome system yet known in nature.ResultsThe organization of the B. cellulosolvens cellulosome is unique compared to previously described cellulosome systems. In contrast to all other known cellulosomes, the cohesin types are reversed for all scaffoldins i.e., the type II cohesins are located on the enzyme-integrating primary scaffoldin, whereas the type I cohesins are located on the anchoring scaffoldins. Many of the type II dockerin-bearing ORFs include X60 modules, which are known to stabilize type II cohesin–dockerin interactions. In the present work, we focused on revealing the architectural arrangement of cellulosome structure in this bacterium by examining numerous interactions between the various cohesin and dockerin modules. In total, we cloned and expressed 43 representative cohesins and 27 dockerins. The results revealed various possible architectures of cell-anchored and cell-free cellulosomes, which serve to assemble distinctive cellulosome types via three distinct cohesin–dockerin specificities: type I, type II, and a novel-type designated R (distinct from type III interactions, predominant in ruminococcal cellulosomes).ConclusionsThe results of this study provide novel insight into the architecture and function of the most intricate and extensive cellulosomal system known today, thereby extending significantly our overall knowledge base of cellulosome systems and their components. The robust cellulosome system of B. cellulosolvens, with its unique binding specificities and reversal of cohesin–dockerin types, has served to amend our view of the cellulosome paradigm. Revealing new cellulosomal interactions and arrangements is critical for designing high-efficiency artificial cellulosomes for conversion of plant-derived cellulosic biomass towards improved production of biofuels.Electronic supplementary materialThe online version of this article (doi:10.1186/s13068-017-0898-6) contains supplementary material, which is available to authorized users.

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“…Substantial advances have been made in recent years [16,59,60,75,95,98,99,[127][128][129][130] and models that are generallyaccepted (at least in gross features) exist for cellulosome structure and function, but the fine details of the molecular mechanisms are still poorly understood. For example, even appended to a CBM, it is not clear how an endoglucanase would be capable of pulling a single polysaccharide chain out of its crystalline environment and forcing the chain productively into its active site cleft.…”

Section: The Role Of Mechanostability In Nanoscale Functionmentioning

confidence: 99%

Nanoscale Engineering of Designer Cellulosomes

et al. 2016

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Biocatalysts showcase the upper limit obtainable for high-speed molecular processing and transformation. Efforts to engineer functionality in synthetic nanostructured materials are guided by the increasing knowledge of evolving architectures, which enable controlled molecular motion and precise molecular recognition. The cellulosome is a biological nanomachine, which, as a fundamental component of the plant-digestion machinery from bacterial cells, has a key potential role in the successful development of environmentally-friendly processes to produce biofuels and fine chemicals from the breakdown of biomass waste. Here, the progress toward so-called "designer cellulosomes", which provide an elegant alternative to enzyme cocktails for lignocellulose breakdown, is reviewed. Particular attention is paid to rational design via computational modeling coupled with nanoscale characterization and engineering tools. Remaining challenges and potential routes to industrial application are put forward.

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Standalone cohesin as a molecular shuttle in cellulosome assembly

Cited by 14 publications

References 41 publications

Enzymatic profiling of cellulosomal enzymes from the human gut bacterium, Ruminococcus champanellensis, reveals a fine‐tuned system for cohesin‐dockerin recognition

Enzymatic profiling of cellulosomal enzymes from the human gut bacterium, Ruminococcus champanellensis, reveals a fine‐tuned system for cohesin‐dockerin recognition

Unique organization and unprecedented diversity of the Bacteroides (Pseudobacteroides) cellulosolvens cellulosome system

Nanoscale Engineering of Designer Cellulosomes

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