A sequence analysis of the β‐glucosidase sub‐family B

Rojas, Antonio; Romeu, Antoni

doi:10.1016/0014-5793(95)01412-8

Cited by 19 publications

(27 citation statements)

References 19 publications

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“…SLW3 had one N-glycosylation site (N-X-S/T) and shared 56% identity with the Trifolium repens cyanogenic ␤-glucosidase (Oxtoby et al, 1991). Similar extents of identity were found with plant ␤-glucosidases that hydrolyze other substrates and belong to the glycosyl hydrolase family 1 (Rojas and Romeu, 1996). The members of this family have been grouped together on the basis of sequence similarities and share two conserved regions ( Figure 10A).…”

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confidence: 88%

Local and Systemic Changes in Squash Gene Expression in Response to Silverleaf Whitefly Feeding

Ven¹,

LeVesque²,

Perring³

et al. 2000

The Plant Cell

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Squash genes ( SLW1 and SLW3 ) induced systemically after silverleaf whitefly feeding were identified. Differences in the local and systemic expression of SLW1 and SLW3 after feeding by the closely related silverleaf and sweetpotato whiteflies were observed. Temporal and spatial studies showed that SLW1 and SLW3 were induced when second, third, and fourth nymphal instars were feeding. Although only barely detected after wounding and bacterial infection, SLW1 and SLW3 RNAs were abundant during water-deficit stress. Treatments with wound/defense signal molecules showed that SLW1 RNAs accumulated in response to methyl jasmonate and ethylene, whereas SLW3 was not regulated by known wound/defense signals, suggesting utilization of a novel mechanism for defense signal transduction. SLW1 RNAs accumulated during floral and fruit development, whereas SLW3 RNAs were not detected during vegetative or reproductive development. The potential roles of SLW1, an M20b peptidase-like protein, and SLW3, a ␤ -glucosidase-like protein, in defense and the leaf-silvering disorder are discussed. INTRODUCTIONAlthough the signal transduction pathways that are activated by mechanical wounding and pathogen invasion have been studied intensively (Ryals et al., 1996;Ryan and Pearce, 1998; Dempsey et al., 1999;Pieterse and van Loon, 1999), there is limited understanding of changes in plant gene expression in response to insect feeding. Given the similarities of mechanical wounding and the damage incurred by insects that masticate foliage, it is not surprising that wound-response transcripts and proteins (i.e., proteinase inhibitors, polyphenol oxidases, and leucine aminopeptidase) accumulate locally and systemically in response to caterpillar feeding (Green and Ryan, 1982;Pautot et al., 1993;Stout et al., 1996; Karban and Baldwin, 1997). However, insect feeding and wounding are not equivalent. Feeding by Manduca sexta larvae, for example, enhances expression of wound-response genes relative to wounding but also induces expression of a novel set of plant genes that are not induced by wounding alone (Korth and Dixon, 1997). Although these herbivory-induced genes have not been identified, some of their gene products may be involved in biosynthesis or release of volatiles that are important in mediating plant-herbivore-predator interactions (Páre and Tumlinson, 1999).Far less is known about the changes in gene expression in response to insects that use other modes of feeding (Stout et al., 1994). Only a few recent studies have investigated plant responses to phloem-feeding whiteflies. Unlike insects that consume foliage, whiteflies do not induce the woundresponse genes that are modulated by the octadecanoid pathway. Whitefly feeding on tomatoes primarily induces the salicylic acid (SA)-independent, jasmonic acid (JA)/ethylene-dependent cascade of defense signal transduction (Chao et al., 1999;Pieterse and van Loon, 1999; D.P. Puthoff and L.L. Walling, manuscript submitted; D.P. Puthoff, C.S. LeVesque, T.M. Perring, and L.L. Walling, manuscript ...

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confidence: 88%

Local and Systemic Changes in Squash Gene Expression in Response to Silverleaf Whitefly Feeding

Ven¹,

LeVesque²,

Perring³

et al. 2000

The Plant Cell

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“…When circularly permuted engineering genes of phosphoribosyl anthranilate isomerase-a singledomain protein that, in its native form, folds as a (␤/␣) 8 -barrel-are expressed in E. coli, the resulting polypeptide products cannot be distinguished from the wild-type protein. 1 More recently, the crystal structures of two circular permutants of the ␣-spectrin SH3 domain were shown to fold into the same 3-D structure as the wild-type, except for the engineered loop that fuses the wild-type termini.…”

Section: Introductionmentioning

confidence: 99%

“…2,3 Proteins derived from naturally occurring genes with apparent circular permutations have been described by several authors. [4][5][6][7][8] Ponting and Russell described circular permutations in the alignment of saposin homologues. 4 Heinemann and Hahn also reported a circular permutation of protein-coding gene sequences in bacterial ␤-glucanases, which adopt the same compact jellyroll fold containing antiparallel ␤-sheets, with amino and carboxyl termini in close proximity.…”

Section: Introductionmentioning

confidence: 99%

“…4 Heinemann and Hahn also reported a circular permutation of protein-coding gene sequences in bacterial ␤-glucanases, which adopt the same compact jellyroll fold containing antiparallel ␤-sheets, with amino and carboxyl termini in close proximity. 5 Since the (␤/␣) 8 -barrel folding configures the structural scaffold of many enzymes, 9 the natural occurrence of cyclic permutants formed by such structural elements is an issue that deserves special attention. The rotational alignments of a number of (␤/␣) 8 barrel-folded proteins showed that some sequences must be cyclically permuted in order to optimize the alignment scores.…”

Section: Introductionmentioning

confidence: 99%

“…The way these elements are linked suggests that there is a double-domain topology made up of a (␤/␣) 8 …”

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Circular permutants in β-glucosidases (family 3) within a predicted double-domain topology that includes a (β/α)8-barrel

Garcı́a-Vallvé¹,

Rojas²,

Palau³

et al. 1998

Proteins

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By predicting the general secondary structure for beta-glucosidases (family 3), in conjunction with existing knowledge of the circular permutants present in B. fibrisolvens and R. albus, we were able to find the canonical elements of the secondary structure. The way these elements are linked suggests that there is a double-domain topology made up of a (beta/alpha)8-barrel domain and a "mainly all-beta" domain. A number of already known conserved motifs are located within (or near) the C-terminal part of the putative parallel beta-strands of the (bet/alpha)8-barrel, which is consistent with what is known about the location of catalytical sites for enzymes that have this domain topology. Within the circular permutants, two beta/alpha units are located at the N-terminal part of the molecule, whereas the other six beta/alpha units are located at the C-terminal end. In this way, the circular permutants can be seen to have a putative discontinuous double-domain topology.

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The quest for alternatives to microbial cellulase mix production: corn stover-produced heterologous multi-cellulases readily deconstruct lignocellulosic biomass into fermentable sugars

Park

Ransom

Mei

et al. 2011

J. Chem. Technol. Biotechnol.

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BACKGROUND: Production of cellulosic ethanol is still expensive compared with corn (maize) grain ethanol due to the high costs of bulk production of microbial cellulases. At least three cellulases including endo-cellulase, exo-cellulase and cellobiase are needed to convert cellulosic biomass into fermentable sugars. All these cellulases could be self-produced within cells of transgenic bio-energy crops. The production of heterologous Acidothermus cellulolyticus (E1) endo-cellulase in endoplasmic reticulum and mitochondria of green tissues of transgenic corn plants was recently reported, and it was confirmed that the heterologous E1 converts cellulose into fermentable sugars.

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A sequence analysis of the β‐glucosidase sub‐family B

Cited by 19 publications

References 19 publications

Local and Systemic Changes in Squash Gene Expression in Response to Silverleaf Whitefly Feeding

Local and Systemic Changes in Squash Gene Expression in Response to Silverleaf Whitefly Feeding

Circular permutants in β-glucosidases (family 3) within a predicted double-domain topology that includes a (β/α)8-barrel

The quest for alternatives to microbial cellulase mix production: corn stover-produced heterologous multi-cellulases readily deconstruct lignocellulosic biomass into fermentable sugars

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