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Hildén, Lars; Daniel, Geoffrey; Johansson, Gunnar

doi:10.1023/a:1022846304826

Cited by 51 publications

(22 citation statements)

References 19 publications

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“…Previous studies have shown that the binding of recombinant Histagged CBMs, at a concentration range of 1-5 g/ml, to plant cell walls can be detected using an indirect triple labeling immunofluorescence procedure (His-tagged CBM, anti-His mouse-Ig, anti-mouse Ig fluorescein isothiocyanate) (27,28). An initial study of CBM binding to transverse sections of a tobacco stem internode (sixth internode from the apex of a 6-week-old tobacco plant) indicated that type A CBMs from families 1, 2a, 3a, and 10, which recognize crystalline cellulose, bound more effectively to cell walls than type B CBMs from families 4-1, 17, and 28, which interact with internal regions of discrete ␤-glucan chains, and the type C CBM from family 9-2, which recognizes the reducing ends of polysaccharides (Fig.…”

Section: Type a Cellulose-directed Cbms Bind More Effectively To Cellmentioning

confidence: 99%

“…The recognition of cellulose in the context of cell walls by diverse families and types of CBM has not been systematically examined. It has been previously demonstrated that CBMs directly coupled to fluorophores or with His tag appendages can be used to investigate the localization of these proteins when bound to target polymers in the context of cell wall composites (27)(28)(29). Here, an immunofluorescence approach is used to interrogate the recognition by type A, B, and C cellulose-directed CBMs (Table 1) of polysaccharides in the context of primary and secondary cell walls in a range of species.…”

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confidence: 99%

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Understanding the Biological Rationale for the Diversity of Cellulose-directed Carbohydrate-binding Modules in Prokaryotic Enzymes

Blake

McCartney

Flint

et al. 2006

Journal of Biological Chemistry

230

167

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Plant cell walls are degraded by glycoside hydrolases that often contain noncatalytic carbohydrate-binding modules (CBMs), which potentiate degradation. There are currently 11 sequence-based cellulose-directed CBM families; however, the biological significance of the structural diversity displayed by these protein modules is uncertain. Here we interrogate the capacity of eight cellulose-binding CBMs to bind to cell walls. These modules target crystalline cellulose (type A) and are located in families 1, 2a, 3a, and 10 (CBM1, CBM2a, CBM3a, and CBM10, respectively); internal regions of amorphous cellulose (type B; CBM4-1, CBM17, CBM28); and the ends of cellulose chains (type C; CBM9-2). Type A CBMs bound particularly effectively to secondary cell walls, although they also recognized primary cell walls. Type A CBM2a and CBM10, derived from the same enzyme, displayed differential binding to cell walls depending upon cell type, tissue, and taxon of origin. Type B CBMs and the type C CBM displayed much weaker binding to cell walls than type A CBMs. CBM17 bound more extensively to cell walls than CBM4-1, even though these type B modules display similar binding to amorphous cellulose in vitro. The thickened primary cell walls of celery collenchyma showed significant binding by some type B modules, indicating that in these walls the cellulose chains do not form highly ordered crystalline structures. Pectate lyase treatment of sections resulted in an increased binding of cellulose-directed CBMs, demonstrating that decloaking cellulose microfibrils of pectic polymers can increase CBM access. The differential recognition of cell walls of diverse origin provides a biological rationale for the diversity of cellulose-directed CBMs that occur in cell wall hydrolases and conversely reveals the variety of cellulose microstructures in primary and secondary cell walls.Cellulose, a major component of plant cell walls and of the biomass of the earth, is a chemically invariant polymer comprising of up to 10,000 ␤-1,4-linked-glucosyl residues. In cell walls cellulose is found in the form of linear insoluble microfibrils that result from self-association of cellulose chains subsequent to synthesis by plasma membrane-located complexes. Biophysical studies have shown that cellulose microfibrils can exist in highly ordered crystalline, semi-ordered para-crystalline, and disordered noncrystalline (amorphous) states (1). Cellulose microfibrils extensively encircle plant cells and are intimately associated with other polysaccharide networks in dense composites that comprise primary and secondary cell walls. The orientation of cellulose microfibrils and their connections with other wall polysaccharide networks are key factors in the generation of cell and organ shapes and mechanical strength during plant growth and development (2).The interactions between cellulose chains both within microfibrils and with matrix polysaccharides within the plant cell wall restrict their accessibility to enzyme attack. To overcome this problem glycoside hydrolas...

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Section: Type a Cellulose-directed Cbms Bind More Effectively To Cellmentioning

confidence: 99%

mentioning

confidence: 99%

Understanding the Biological Rationale for the Diversity of Cellulose-directed Carbohydrate-binding Modules in Prokaryotic Enzymes

Blake

McCartney

Flint

et al. 2006

Journal of Biological Chemistry

230

167

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“…This might perhaps partly explain the different results obtained. Other non-CLSM fluorescence microscopy studies showing enzymes binding to dislocations involved CBMs that were not used in our study (CBM3 and CBM28 of Clostridium josui on Japan cedar wood (Kawakubo et al 2010 ), CBM6 of Clostridium thermocellum on Valonia ventricusa cellulose (Ding et al 2006 ), CBM1 from Phanerochaete chrysoporum Cel7D on delignified spruce/birch pulp fibers [Hildén et al 2003 ]). Recently, swollenin has also been shown, by use of CLSM combined with other techniques, to target and disrupt dislocations (Gourlay et al 2015 ).…”

Section: Discussionmentioning

confidence: 86%

“…The use of CLSM differs from traditional binding studies (e.g. Filonova et al 2007 ; Hildén et al 2003 ) where the amount of bound enzyme is estimated based on what is present in the supernatant after a certain incubation period, giving no information on the location of the bound enzymes.…”

Section: Introductionmentioning

confidence: 99%

The binding of cellulase variants to dislocations: a semi-quantitative analysis based on CLSM (confocal laser scanning microscopy) images

Hidayat¹,

Weisskopf

Felby

et al. 2015

AMB Expr

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Binding of enzymes to the substrate is the first step in enzymatic hydrolysis of lignocellulose, a key process within biorefining. During this process elongated plant cells such as fibers and tracheids have been found to break into segments at irregular cell wall regions known as dislocations or slip planes. Here we study whether cellulases bind to dislocations to a higher extent than to the surrounding cell wall. The binding of fluorescently labelled cellobiohydrolases and endoglucanases to filter paper fibers was investigated using confocal laser scanning microscopy and a ratiometric method was developed to assess and quantify the abundance of the binding of cellulases to dislocations as compared to the surrounding cell wall. Only Humicola insolens EGV was found to have stronger binding preference to dislocations than to the surrounding cell wall, while no difference in binding affinity was seen for any of the other cellulose variants included in the study (H. insolens EGV variants, Trichoderma reesei CBHI, CBHII and EGII). This result favours the hypothesis that fibers break at dislocations during the initial phase of hydrolysis mostly due to mechanical failure rather than as a result of faster degradation at these locations.

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“…5) Recently, such labeled CBMs have been used as molecular probes to study the architecture of plant cell walls. [5][6][7][8] The endoglucanase Cel5A from Clostridium josui contains a family 17 CBM (CjCBM17) and a family 28 CBM (CjCBM28) in tandem. 9) Both family 17 and family 28 CBMs from C. josui are type B CBMs.…”

mentioning

confidence: 99%

Family 17 and 28 Carbohydrate-Binding Modules Discriminated Different Cell-Wall Sites in Sweet Potato Roots

Araki

Karita

Kondo

et al. 2010

Bioscience, Biotechnology, and Biochemistry

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Untitled

Cited by 51 publications

References 19 publications

Understanding the Biological Rationale for the Diversity of Cellulose-directed Carbohydrate-binding Modules in Prokaryotic Enzymes

Understanding the Biological Rationale for the Diversity of Cellulose-directed Carbohydrate-binding Modules in Prokaryotic Enzymes

The binding of cellulase variants to dislocations: a semi-quantitative analysis based on CLSM (confocal laser scanning microscopy) images

Family 17 and 28 Carbohydrate-Binding Modules Discriminated Different Cell-Wall Sites in Sweet Potato Roots

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