Origin, distribution and 3D‐modeling of Gr‐EXPB1, an expansin from the potato cyst nematode <i>Globodera rostochiensis</i>

Kudla, U.; Qin, Ling; Milac, Adina L.; Kielak, Anna M.; Maissen, Cyril; Overmars, H.A.; Popeijus, Herman E.; Roze, E.H.A.; Petrescu, Andrei‐Jose; Smant, G.; Bakker, J.; Helder, J.

doi:10.1016/j.febslet.2005.03.047

Cited by 63 publications

(47 citation statements)

References 28 publications

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“…In addition, genomic DNA sequences of Bx-EXPBs showed that Bx-EXPBs likey did not originate from endogenous or symbiotic microorganisms. BLAST search and genomic DNA sequence of Bx-EXPBs led to suggestion that Bx-EXPBs could have originated from bacteria via horizontal gene transfer as shown in other cell wall degrading enzymes and biologically functional (Jones et al, 2005;Kudla et al, 2005;Scholl et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

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Identification and Characterization of Expansins from Bursaphelenchus xylophilus (Nematoda: Aphelenchoididae)

Lee¹,

Seo²,

Kang³

et al. 2012

The Plant Pathology Journal

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We identified two novel expansin (EXP) genes in the expressed sequence tag database of Bursaphelenchus xylophilus, designated as Bx-EXPB2 and -EXPB3. Novel Bx-EXPBs encoded 150 amino acids and their similarities in coding sequence were 70.7−84.0% to the previously reported EXPB1 of B. xylophilus. Bx-EXPB2 and Bx-EXPB3 were clustered with Bx-EXPB1 and Bm-EXPB1, respectively, forming the independent phylogeny with other nematode EXPs. All identified Bx-EXPBs contained the signal peptide and were only expressed during the propagative stage, suggesting that they are secreted to facilitate nematode migration through hosts by loosening cell walls during infection. Quantitative real-time PCR analysis showed that the relative accumulation of Bx-EXPB3 mRNAs was the highest among the three Bx-EXPs examined and the order of mRNA accumulation was as follows: Bx-EXPB3 > Bx-EXPB2 >> Bx-EXPB1. Homology modeling of BxEXPBs showed that the structurally optimum template was EXLX1 protein of Bacillus subtilis, whichshared residues essential for catalytic activity with Bx-EXPB1 and Bx-EXPB2 except for Bx-EXPB3. Taken together, Bx-EXPB1 and Bx-EXPB2 may be involved migration through plant tissues and play a role in pathogenesis.

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Section: Discussionmentioning

confidence: 99%

“…The EG45-like domain found in diverse EXP-related proteins (Kudla et al, 2005;Li et al, 2002;Xu et al, 2001) has multiple cysteine/tryptophan residues and conserved HFD amino acid sequence motif. Non-plant EXPs including nematode EXPs may have evolved independently of plant EXPs leading to the different gene structure.…”

Section: Discussionmentioning

confidence: 99%

Identification and Characterization of Expansins from Bursaphelenchus xylophilus (Nematoda: Aphelenchoididae)

Lee¹,

Seo²,

Kang³

et al. 2012

The Plant Pathology Journal

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“…Expansins are ~27 kDa and ~225 aa proteins consisting of two compact domains: the N-terminal, which resembles the catalytic domain of family 45 glycoside hydrolases (GH45); and the C-terminal, which has been reported as a cellulose-binding domain (Yennawar et al, 2006). Expansin genes appear to be highly conserved throughout plant evolution, but proteins remarkably similar to plant expansin sequences have also been found in Dictyostelium discoideum, (Li et al, 2002), nematodes (Qin et al, 2004;Kudla et al, 2005;Fudali et al, 2008), the ascomycete fungi Trichoderma reesii (Saloheimo et al, 1994), mussels (Xu et al, 2001) and the bacterium Bacillus subtilis (Kerff et al, 2008). The expansin-like sequences in bacteria, animals and fungi appear to be restricted to organisms involved in plant pathogenesis or plant cell wall digestion (Li et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Immunolocalization of α-Expansin Protein (NtEXPA5) in Tobacco Roots in the Presence of the Arbuscular Mycorrhizal Fungus Glomus Mosseae Nicol. & Gerd

Wiśniewska¹,

Golinowski²

2011

Acta Biologica Cracoviensia Series Botanica

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The arbuscules of mycorrhizae develop within apoplastic compartments of the host plant, as they are separated from the cell protoplast by an interfacial matrix continuous with the plant cell wall. Expansins are proteins that allow cell wall loosening and extension. Using fluorescence and electron microscopy we located the NtEXPA5 epitopes recognized by polyclonal antibody anti-NtEXPA5 in mycorrhizal tobacco roots. The expansin protein was localized mainly within the interfacial matrix of intracellular hyphae, arbuscule trunk and main branches. NtEXPA5 proteins were detected neither within the interface of collapsing arbuscule branches nor in non-colonized cortex cells. In plant cell walls, expansin protein was detected only at the penetration point and in the parts of cell walls that adhered firmly to fungal hyphae growing intracellularly. For the first time, NtEXPA5 protein was localized ultrastructurally in hyphae growing intracellularly at the interface of the hypha tip and sites of bending. The novel localization of NtEXPA5 protein suggests that this protein may be involved in the process of arbuscule formation: that is, in promoting apical hyphal growth and arbuscule ramification, as well as in controlling the dynamic of arbuscule mycorrhiza development.K Ke ey y w wo or rd ds s: : Arbuscular mycorrhizae, arbuscule, expansin, host/fungus interface, ultrastructure.

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“…In the phylum Nematodea, CBMs have been found in secretions of the root knot nematode Meloidogyne incognita (51) and in the soybean cyst nematode Heterodera glycines (65), and recently it was demonstrated that nematodes express expansin during plant feeding (110,159).…”

Section: Introductionmentioning

confidence: 99%

Carbohydrate Binding Modules: Biochemical Properties and Novel Applications

Shoseyov

Shani

Levy

2006

Microbiol Mol Biol Rev

490

347

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SUMMARY Polysaccharide-degrading microorganisms express a repertoire of hydrolytic enzymes that act in synergy on plant cell wall and other natural polysaccharides to elicit the degradation of often-recalcitrant substrates. These enzymes, particularly those that hydrolyze cellulose and hemicellulose, have a complex molecular architecture comprising discrete modules which are normally joined by relatively unstructured linker sequences. This structure is typically comprised of a catalytic module and one or more carbohydrate binding modules (CBMs) that bind to the polysaccharide. CBMs, by bringing the biocatalyst into intimate and prolonged association with its substrate, allow and promote catalysis. Based on their properties, CBMs are grouped into 43 families that display substantial variation in substrate specificity, along with other properties that make them a gold mine for biotechnologists who seek natural molecular “Velcro” for diverse and unusual applications. In this article, we review recent progress in the field of CBMs and provide an up-to-date summary of the latest developments in CBM applications.

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Origin, distribution and 3D‐modeling of Gr‐EXPB1, an expansin from the potato cyst nematode Globodera rostochiensis

Cited by 63 publications

References 28 publications

Identification and Characterization of Expansins from Bursaphelenchus xylophilus (Nematoda: Aphelenchoididae)

Identification and Characterization of Expansins from Bursaphelenchus xylophilus (Nematoda: Aphelenchoididae)

Immunolocalization of α-Expansin Protein (NtEXPA5) in Tobacco Roots in the Presence of the Arbuscular Mycorrhizal Fungus Glomus Mosseae Nicol. & Gerd

Carbohydrate Binding Modules: Biochemical Properties and Novel Applications

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