Substrate-binding domains of glycanases from Streptomyces lividans: characterization of a new family of xylan-binding domains

Dupont, Claude; Roberge, Martin; Shareck, François; Morosoli, Rolf; Kluepfel, Dieter

doi:10.1042/bj3300041

Cited by 48 publications

(40 citation statements)

References 27 publications

(32 reference statements)

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“…Tomme et al (1995) divide the CBD II family into CBD IIa and CBD IIb, the latter having a C-terminal deletion covering an otherwise conserved Trp residue. On this criterion, the CBD domains of Hoglet-N are in the CBD IIb subfamily (also called XBD, xylanbinding domains, reflecting binding specificity of some domains; Dupont et al 1998). …”

Section: Resultsmentioning

confidence: 99%

An unusual choanoflagellate protein released by Hedgehog autocatalytic processing

Snell

Brooke

Taylor³

et al. 2005

Proc. R. Soc. B.

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Hedgehog proteins are important cell-cell signalling proteins utilized during the development of multicellular animals. Members of the hedgehog gene family have not been detected outside the Metazoa, raising unanswered questions about their evolutionary origin. Here we report a highly unusual hedgehog-related gene from a choanoflagellate, a close unicellular relative of the animals. The deduced C-terminal domain, Hoglet-C, is homologous to the autocatalytic domain of Hedgehog proteins and is predicted to function in autocatalytic cleavage of the precursor peptide. In contrast, the N-terminal Hoglet-N peptide has no similarity to the signalling peptide of Hedgehog (Hh-N). Instead, Hoglet-N is deduced to be a secreted protein with an enormous threonine-rich domain of unprecedented size and purity (over 200 threonine residues) and two polysaccharide-binding domains. Structural modelling reveals that these domains have a novel combination of features found in cellulose-binding domains (CBD) of types IIa and IIb, and are expected to bind cellulose. We propose that the two CBD domains enable Hoglet-N to bind to plant matter, tethering an amorphous nucleophilic anchor, facilitating transient adhesion of the choanoflagellate cell. Since Hh-C and Hoglet-C are homologous, but Hh-N and Hoglet-N are not, we argue that metazoan hedgehog genes evolved by fusion of two distinct genes.

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Section: Resultsmentioning

confidence: 99%

An unusual choanoflagellate protein released by Hedgehog autocatalytic processing

Snell

Brooke

Taylor³

et al. 2005

Proc. R. Soc. B.

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“…However, this type CBM6 module had highest affinity for xylan, and bound only weakly to Avicel and acid-swollen cellulose. Dupont et al (1998) have shown that the Streptomyces lividans xylanases AxeA and XlnB possess the family 2 of carbohydrate-binding modules, which specifically bind insoluble xylan and do not bind cellulose. The modular structure of xylanase of A. pushchinoensis A8 is a future task of ongoing studies to determine its entire gene sequence.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a xylanase from a thermophilic strain of Anoxybacillus pushchinoensis A8

et al. 2008

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A facultatively anaerobic, thermophilic, xylanolytic bacterium was isolated from a sample collected from the Diyadin Hot Springs, Turkey. According to morphological, biochemical and molecular identification, this new strain was suggested to be representative of the Anoxybacillus pushchinoensis and it was designated as Anoxybacillus pushchinoensis strain A8. It exhibited 97% similarity to 16S rRNA gene sequence of A. pushchinoensis and 77% DNA homology by DNA-DNA hybridization studies. Q-sepharose and CM-sepharose chromatography was used to purify an extracellular xylanase to >90% purity from this species. The enzyme had a molecular mass of approximately 83 kDa. The enzyme showed optimum activity at pH 6.5 and it was 96% stable over a broad pH range of 6.5-11 for 24 hours. The enzyme had optimum activity at 55• C and it was 100% stable at temperature between 50-60• C up to 24 hours. Kinetic characterization of the enzyme was performed at temperature optima (55 • C) and Vmax and Km were found to be 59.88 U/mg protein and 0.909 mg/mL, respectively. Oat spelt xylan but not xylooligosaccharides was degraded by the enzyme and xylose was the only product detected from oat xylan degradation. This suggested that the enzyme was an exo-acting xylanase.

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“…The N-terminal region of Xyn5 containing family 22 CBMs (i.e., CBM22-1 and CBM22-2), extending from positions 43 to 365 (numbered from the initial Met of the polypeptide encoded by xyn5), have sequence similarity with the family 22 CBMs of C. josui Xyn10A, Clostridium stercorarium Xyn10B, C. thermocellum Xyn10B, Clostridium fini XynC, Thermotoga maritima Xyn10A, and Thermoanaerobacterium saccharolyticum XynA (i.e., the sequence identities between the family 22 CBMs of Xyn5 and those of the other xylanases are 46.8 to 21.9%). It has been shown that the family 22 CBM of T. maritima Xyn10A and several other family 10 xylanases have the ability to bind soluble xylan (3,8,10,18) and that the family 22 CBMs of T. maritima Xyn10A and T. saccharolyticum XynA contribute to the heat stability of these enzymes (15,18,35). The family 10 catalytic domain of Xyn5, extending from positions 370 to 712 (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…In addition to the cellulose-binding activity, Xyn5 would have xylan-binding activity because of the presence of the family 22 CBMs. It has been shown that family 22 CBMs of T. maritima Xyn10A and C. thermocellum Xyn10B have xylanbinding and thermostabilizing functions (3,8,10,15,18,35 is replaced with another aromatic amino acid, Tyr. In addition, CBM22-2 of Xyn5 has 28.2% amino acid sequence identity with C. thermocellum Xyn10B.…”

Section: Discussionmentioning

confidence: 99%

Cloning, Expression, and Cell Surface Localization of Paenibacillus sp. Strain W-61 Xylanase 5, a Multidomain Xylanase

Ito

Tomita

Roy

et al. 2003

Appl Environ Microbiol

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We have shown that a xylan-degrading bacterium, W-61, excretes multiple xylanases, including xylanase 5 with a molecular mass of 140 kDa. Here, we emend the previously used classification of the bacterium (i.e., Aeromonas caviae W-61) to Paenibacillus sp. strain W-61 on the basis of the nucleotide sequence of the 16S rRNA gene, and we clone and express the xyn5 gene encoding xylanase 5 (Xyn5) in Escherichia coli and study the subcellular localization of Xyn5. xyn5 encodes 1,326 amino acid residues, including a 27-amino-acid signal sequence. Sequence analysis indicated that Xyn5 comprises two family 22 carbohydrate-binding modules (CBM), a family 10 catalytic domain of glycosyl hydrolases, a family 9 CBM, a domain similar to the lysine-rich region of Clostridium thermocellum SdbA, and three S-layer-homologous (SLH) domains. Recombinant Xyn5 bound to a crystalline cellulose, Avicel PH-101, while an N-terminal 90-kDa fragment of Xyn5, which lacks the C-terminal half of the family 9 CBM, did not bind to Avicel PH-101. Xyn5 was cell bound, and the cell-bound protein was digested by exogenous trypsin to produce immunoreactive and xylanolytic fragments with molecular masses of 80 and 60 kDa. Xyn5 was exclusively distributed in the cell envelope fraction consisting of a peptidoglycan-containing layer and an associated S layer. Thus, Paenibacillus sp. strain W-61 Xyn5 is a cell surface-anchored modular xylanase possessing a functional cellulose-binding module and SLH domains. Possible cooperative action of multiple xylanases produced by strain W-61 is discussed on the basis of the modular structure of Xyn5.

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Substrate-binding domains of glycanases from Streptomyces lividans: characterization of a new family of xylan-binding domains

Cited by 48 publications

References 27 publications

An unusual choanoflagellate protein released by Hedgehog autocatalytic processing

An unusual choanoflagellate protein released by Hedgehog autocatalytic processing

Characterization of a xylanase from a thermophilic strain of Anoxybacillus pushchinoensis A8

Cloning, Expression, and Cell Surface Localization of Paenibacillus sp. Strain W-61 Xylanase 5, a Multidomain Xylanase

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