Identification and Characterization of a Xyloglucan-Specific Family 74 Glycosyl Hydrolase from Streptomyces coelicolor A3(2)

Enkhbaatar, Bolormaa; Temuujin, Uyangaa; Lim, Jae-Hwan; Chi, Won-Jae; Chang, YongKeun; Hong, Soon-Kwang

doi:10.1128/aem.06482-11

Cited by 28 publications

(14 citation statements)

References 26 publications

(19 reference statements)

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“…5A). Compared to known functionally characterized GH74 xyloglucanases, which have K m values in the range 0.25-1.2 mgÁmL À1 for tamarind seed XyG, the K m value of CjGH74 is notably low [38,39,45,[48][49][50]. Moreover, the turnover number of CjGH74 is among the highest observed for previously characterized GH74 endo-xyloglucanases, which emphasizes the…”

Section: Cjgh74 Substrate Specificitymentioning

confidence: 92%

“…1) to generate the oligosaccharides XXXG, XLXG, XXLG and XLLG, which differ in their degree of side-chain galactosylation (Figs 6 and 7). This is the most common cleavage pattern observed for GH74 endo-xyloglucanases [38,41,[48][49][50], although certain members are known to cleave between branched backbone glucosyl units [42,43,51,52].…”

Section: Bond Cleavage Specificity and Mode Of Action Of Cjgh74mentioning

confidence: 99%

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Functional and structural characterization of a potent GH74 endo‐xyloglucanase from the soil saprophyte Cellvibrio japonicus unravels the first step of xyloglucan degradation

et al. 2016

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The heteropolysaccharide xyloglucan (XyG) comprises up to one‐quarter of the total carbohydrate content of terrestrial plant cell walls and, as such, represents a significant reservoir in the global carbon cycle. The complex composition of XyG requires a consortium of backbone‐cleaving endo‐xyloglucanases and side‐chain cleaving exo‐glycosidases for complete saccharification. The biochemical basis for XyG utilization by the model Gram‐negative soil saprophytic bacterium Cellvibrio japonicus is incompletely understood, despite the recent characterization of associated side‐chain cleaving exo‐glycosidases. We present a detailed functional and structural characterization of a multimodular enzyme encoded by gene locus CJA_2477. The CJA_2477 gene product comprises an N‐terminal glycoside hydrolase family 74 (GH74) endo‐xyloglucanase module in train with two carbohydrate‐binding modules (CBMs) from families 10 and 2 (CBM10 and CBM2). The GH74 catalytic domain generates Glc4‐based xylogluco‐oligosaccharide (XyGO) substrates for downstream enzymes through an endo‐dissociative mode of action. X‐ray crystallography of the GH74 module, alone and in complex with XyGO products spanning the entire active site, revealed a broad substrate‐binding cleft specifically adapted to XyG recognition, which is composed of two seven‐bladed propeller domains characteristic of the GH74 family. The appended CBM10 and CBM2 members notably did not bind XyG, nor other soluble polysaccharides, and instead were specific cellulose‐binding modules. Taken together, these data shed light on the first step of xyloglucan utilization by C. japonicus and expand the repertoire of GHs and CBMs for selective biomass analysis and utilization. Database Structural data have been deposited in the RCSB protein database under the Protein Data Bank codes: http://www.rcsb.org/pdb/search/structidSearch.do?structureId=5FKR, http://www.rcsb.org/pdb/search/structidSearch.do?structureId=5FKS, http://www.rcsb.org/pdb/search/structidSearch.do?structureId=5FKT and http://www.rcsb.org/pdb/search/structidSearch.do?structureId=5FKQ.

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Section: Cjgh74 Substrate Specificitymentioning

confidence: 92%

Section: Bond Cleavage Specificity and Mode Of Action Of Cjgh74mentioning

confidence: 99%

Functional and structural characterization of a potent GH74 endo‐xyloglucanase from the soil saprophyte Cellvibrio japonicus unravels the first step of xyloglucan degradation

et al. 2016

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“…Among bacteria, the members of the phylum Actinobacteria show the highest abundance of genes involved in cellulose decomposition in their genomes (Berlemont and Martiny 2013), and many isolates have been shown to be able to efficiently degrade polysaccharides and polyphenols (Abdulla and El-Shatoury 2007;Anderson et al 2012;Chater et al 2010;Enkhbaatar et al 2012;Větrovský et al 2014;Yin et al 2010). Bulk lignocellulose materials are more accessible for decomposition by filamentous microorganisms such as fungi and Actinobacteria (de Boer et al 2005), and efficient growth on straw was indeed demonstrated for environmental isolates of Actinobacteria (Větrovský et al 2014).…”

Section: Introductionmentioning

confidence: 91%

An in-depth analysis of actinobacterial communities shows their high diversity in grassland soils along a gradient of mixed heavy metal contamination

Větrovský

Baldrián

2015

Biol Fertil Soils

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Several previous studies indicated that Actinobacteria may be enriched in soils with elevated content of heavy metals. In this study, we have developed a method for the in-depth analysis of actinobacterial communities in soil through phylum-targeted high-throughput sequencing and used it to address this question and examine the community composition in grassland soils along a gradient of heavy metal contamination (Cu, Zn, Cd, Pb). The use of the 16Sact111r primer specific for Actinobacteria resulted in a dataset obtained by pyrosequencing where over 98 % of the sequences belonged to Actinobacteria. The diversity within the Actinobacterial community was not affected by the heavy metals, but the contamination was the most important factor affecting community composition. The most significant changes in community composition were due to the content of Cu and Pb, while the effects of Zn and Cd were relatively minor. For the most abundant actinobacterial taxa, the abundance of taxa identified as members of the genera Acidothermus, Streptomyces, Pseudonocardia, Janibacter and Microlunatus increased with increasing metal content, while t hose belonging to Jatrophihabitans and Actinoallomurus decreased. The genus Ilumatobacter contained operational taxonomic units (OTUs) that responded to heavy metals both positively and negatively. This study also confirmed that Actinobacteria appear to be less affected by heavy metals than other bacteria. Because several Actinobacteria were also identified in playing a significant role in cellulose and lignocellulose decomposition in soil, they potentially represent important decomposers of organic matter in such environments.

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“…KM21, and Phanerochaete chrysosporium (15,22,35). The Streptomyces coelicolor A(3) xyloglucanase Sco6545, belonging to the GH74 family, was recently cloned and characterized (9). The deduced amino acid sequence of Sco6545 was found to be similar to that of SaGH74A.…”

Section: Discussionmentioning

confidence: 90%

“…In contrast, two or more genes classified as members of the GH74 family in the CAZy database are present in many bacteria. Streptomyces species are the most extensively studied of these bacteria and have been used as a source of hemicellulases (2,4,9,12,19,20,23,28,32). Streptomyces avermitilis possesses two GH74 genes, which are similar to those found in Geotrichum sp.…”

mentioning

confidence: 83%

Characterization of an Endo-Processive-Type Xyloglucanase Having a β-1,4-Glucan-Binding Module and an Endo-Type Xyloglucanase from Streptomyces avermitilis

Ichinose

Araki

Michikawa

et al. 2012

Appl Environ Microbiol

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e We cloned two glycoside hydrolase family 74 genes, the sav_1856 gene and the sav_2574 gene, from Streptomyces avermitilis NBRC14893 and characterized the resultant recombinant proteins. The sav_1856 gene product (SaGH74A) consisted of a catalytic domain and a family 2 carbohydrate-binding module at the C terminus, while the sav_2574 gene product (SaGH74B) consisted of only a catalytic domain. SaGH74A and SaGH74B were expressed successfully and had molecular masses of 92 and 78 kDa, respectively. Both recombinant proteins were xyloglucanases. SaGH74A had optimal activity at 60°C and pH 5.5, while SaGH74B had optimal activity at 55°C and pH 6.0. SaGH74A was stable over a broad pH range (pH 4.5 to 9.0), whereas SaGH74B was stable over a relatively narrow pH range (pH 6.0 to 6.5). Analysis of the hydrolysis products of tamarind xyloglucan and xyloglucan-derived oligosaccharides indicated that SaGH74A was endo-processive, while SaGH74B was a typical endo-enzyme. The C terminus of SaGH74A, which was annotated as a carbohydrate-binding module, bound to ␤-1,4-linked glucan-containing soluble polysaccharides such as hydroxyethyl cellulose, barley glucan, and xyloglucan.

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Identification and Characterization of a Xyloglucan-Specific Family 74 Glycosyl Hydrolase from Streptomyces coelicolor A3(2)

Cited by 28 publications

References 26 publications

Functional and structural characterization of a potent GH74 endo‐xyloglucanase from the soil saprophyte Cellvibrio japonicus unravels the first step of xyloglucan degradation

Functional and structural characterization of a potent GH74 endo‐xyloglucanase from the soil saprophyte Cellvibrio japonicus unravels the first step of xyloglucan degradation

An in-depth analysis of actinobacterial communities shows their high diversity in grassland soils along a gradient of mixed heavy metal contamination

Characterization of an Endo-Processive-Type Xyloglucanase Having a β-1,4-Glucan-Binding Module and an Endo-Type Xyloglucanase from Streptomyces avermitilis

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