Characterization of two membrane-associated <i>β</i>-glucosidases from maize (<i>Zea mays</i> L.) coleoptiles

Vente, Andreas; Zettl, Rolf; Bako, L.; Campos, Narciso; Palme, Klaus

doi:10.1042/bj3020015

Cited by 11 publications

(7 citation statements)

References 29 publications

(26 reference statements)

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“…Feldwisch et al used an azido derivative of IAA to identify auxin-binding proteins of MW 2 3 , 24-, 58-, and 60-kD (30). The 23-kD protein, called pm23 is recognized by an antisera directed against ABP-1.…”

Section: Auxin Receptorsmentioning

confidence: 99%

The plant hormone auxin: Insight in sight

Estelle

1992

BioEssays

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Physiological experiments conducted over the last 60 years indicate that the plant hormone auxin regulates a diverse set of developmental processes via changes in cell division, cell elongation and cell differentiation. Recent studies using transgenic plants with altered auxin levels support these conclusions and promise to provide more detailed information on the role of auxin during plant development. Although it is possible that all auxin responses are mediated by the same primary biochemical events, the studies described in this review are more consistent with multiple modes of auxin action. The development of molecular and genetic approaches to the study of hormone action should resolve this issue. The accelerated rate of progress in this field suggests that real insight into the mechanism of auxin action may be forthcoming.

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Section: Auxin Receptorsmentioning

confidence: 99%

The plant hormone auxin: Insight in sight

Estelle

1992

BioEssays

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“…The maize enzyme that can be extracted from young coleoptiles hydrolyzes DIM-BOA-Glc and other aryl or alkyl b-D-glucosides (Esen 1992;Babcock and Esen 1994;Czjzek et al 2001). It can also hydrolyse auxin-glucosides and other hormones (Campos et al 1992;Campos et al 1993;Feldwisch et al 1994). The b-glucosidase enzyme (BGLU) is often compartmentalized at the subcellular level (either in the plastid, cytosol, vacuole or apoplast) and can be found mainly in young vegetative parts (Kristoffersen et al 2000;Biely et al 2003).…”

Section: Introductionmentioning

confidence: 99%

Genome-wide analysis of the beta-glucosidase gene family in maize (Zea mays L. var B73)

Goméz‐Anduro¹,

Ceniceros-Ojeda²,

Casados‐Vázquez³

et al. 2011

Plant Mol Biol

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The hydrolysis of beta-D: -glucosidic bonds which is required for the liberation of many physiologically important compounds is catalyzed by the enzyme beta-glucosidase (BGLU, EC 3.2.1.21). BGLUs are implicated in several processes in plants, such as the timely response to biotic and abiotic stresses through activation of phytohormones and defense compounds. We identified 26 BGLU isozymes in the genome of the maize inbred B73 and propose a standardized nomenclature for all Zea mays BGLU paralogs (Zmbglu1-Zmbglu26). We characterized their intron-exon structure, protein features, phylogenetic relationships, and measured their expression and activity in various tissues under different environmental conditions. Sequence alignments revealed some characteristic motifs (conserved amino acids) and specific differences among different isozymes. Analysis of putative signal peptides suggested that some BGLUs are plastidic, whereas others are mitochondrial, cytosolic, vacuolar or secreted. Microarray and RT-PCR analysis showed that each member of the Zmbglu family had a characteristic expression pattern with regard to tissue specificity and response to different abiotic conditions. The source of variance for gene expression was highest for the type of organ analyzed (tissue variance) than for the growth conditions (environmental variance) or genotype (genetic variance). Analysis of promoter sequences revealed that each Zmbglu paralog possesses a distinct set of cis elements and transcription factor binding sites. Since there are no two Zmbglu paralogs that have identical molecular properties, we conclude that gene subfunctionalization in maize occurs much more rapidly than gene duplication.

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“…Fractions with higher β-glucosidase activity were pooled. ParsBgl showed very high activity compared to previously reported β-glucosidases from Zea mays L. (6.24 U/mg), Prunus avium L. (27.49 U/mg), and corn stover (18.6 U/mg) [8,9,12].…”

Section: Purification Of Parsbglmentioning

confidence: 51%

“…[8][9][10][11][12][13][14][15][16][17]. In plants, this enzyme plays a role in several metabolic processes [18].…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of cyanogenic β-glucosidase from wild apricot (Prunus armeniaca L.)

Bhalla

Asif

Smita

2017

Process Biochemistry

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Characterization of two membrane-associated β-glucosidases from maize (Zea mays L.) coleoptiles

Cited by 11 publications

References 29 publications

The plant hormone auxin: Insight in sight

The plant hormone auxin: Insight in sight

Genome-wide analysis of the beta-glucosidase gene family in maize (Zea mays L. var B73)

Purification and characterization of cyanogenic β-glucosidase from wild apricot (Prunus armeniaca L.)

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