An Invertase Inactivator in Maize Endosperm and Factors Affecting Inactivation

Jaynes, T. A.; Nelson, Oliver E.

doi:10.1104/pp.47.5.629

Cited by 57 publications

(28 citation statements)

References 10 publications

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“…Invertase inhibitor proteins were first characterized biochemically as copurifying proteins in invertase enzyme preparations (Pressey, 1966;Jaynes and Nelson, 1971) and dicot genes encoding INVINH proteins with demonstrated activity in vitro and in vivo (Greiner et al, 1999) were recently characterized. Analysis of sequences from maize and other monocots indicates that there are at least two to three INVINH-related proteins in these species as well.…”

Section: Discussionmentioning

confidence: 99%

“…Protein was quantified by Bradford reagent (Bio-Rad Laboratories, Hercules, CA). Invertase activity was measured by adapting a protocol of the Nelson's assay (Jaynes and Nelson, 1971) for 96-well plates. Fifty microliters of soluble or insoluble enzyme preparation was incubated with 2% (w/v) Suc at 37°C for 30 min before transfer to Somagyi's reagent and heating to 100°C for 10 min.…”

Section: Recombinant Protein Expression and Invertase Activitymentioning

confidence: 99%

“…In addition, small (Ͻ20-kD) inhibitor proteins (INVINH) have been associated with invertase preparations in a number of dicot plant species (Pressey, 1994;Weil et al, 1994;Krausgrill et al, 1996Krausgrill et al, , 1998Greiner et al, 1998Greiner et al, , 2000 since their first biochemical characterization (Pressey, 1966;Jaynes and Nelson, 1971). Recently, the first gene encoding an INVINH was characterized from tobacco (Nicotiana tabacum) and was shown to have inhibitory activity by assaying the effect of recombinant protein on invertase activity in vitro .…”

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An Invertase Inhibitor from Maize Localizes to the Embryo Surrounding Region during Early Kernel Development

et al. 2004

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Invertase activity is thought to play a regulatory role during early kernel development by converting sucrose originating from source leaves into hexoses to support cell division in the endosperm and embryo. Invertases are regulated at the posttranslational level by small protein inhibitors, INVINHs. We found that in maize (Zea mays), an invertase inhibitor homolog (ZM-INVINH1) is expressed early in kernel development, between 4 and 7 d after pollination. Invertase activity is reduced in vitro in the presence of recombinant ZM-INVINH1, and inhibition is attenuated by pre-incubation with sucrose. The presence of a putative signal peptide, fractionation experiments, and ZM-INVINH1::green fluorescent protein fusion experiments indicate that the protein is exported to the apoplast. Moreover, association of ZM-INVINH1 with the glycoprotein fraction by concanavalin A chromatogaphy suggests that ZM-INVINH1 interacts with an apoplastic invertase during early kernel development. ZM-INVINH1 was localized to the embryo surrounding region by in situ analysis, suggesting that this region forms a boundary, compartmentalizing apoplast invertase activity to allow different embryo and endosperm developmental rates.Kernel development in maize (Zea mays) proceeds through a series of tightly regulated, overlapping stages. After double fertilization, during the prestorage phase, two distinct cell types are established: the triploid endosperm and the diploid embryo. Despite clearly different cell fates, the embryo and endosperm both rely upon photosynthate from source leaves transported through the maternal pedicel region of the developing kernel, ending at the terminal phloem cells. The presence of Suc-hydrolyzing enzymes, which produce hexose sugars from Suc, have been identified as critical for the establishment of the prestorage phase of seed development, and Suc hydrolysis is an important component of realizable plant yield (Cheng and Chourney, 1999;Weschke et al., 2003). The "invertase control hypothesis," largely based on work from dicots (Wobus and Weber, 1999), is supported in maize by the presence of a cell wall invertase, INCW2, localized to the basal endosperm transfer layer (Talercio et al., 1999). Mutations in this gene result in miniature kernels (the mn1 mutation) and have a severely reduced endosperm (Cheng et al., 1996;Vilhar et al., 2002). Recently, the association of a IVR2, a soluble invertase expressed during early kernel development, with seed yield under conditions of limiting photosynthesis suggests that soluble invertases also play a significant role in providing hexose sugars to support cell division during the prestorage phase (Andersen et al., 2002), as has been previously suggested (Zinselmeier et al., 1999).Invertases exhibit complex regulation at the transcriptional and posttranscriptional levels in response to developmental, environmental, and carbohydrate signals (Sturm, 1999). In addition, small (Ͻ20-kD) inhibitor proteins (INVINH) have been associated with invertase preparations in a number of dico...

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Section: Discussionmentioning

confidence: 99%

Section: Recombinant Protein Expression and Invertase Activitymentioning

confidence: 99%

mentioning

confidence: 99%

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An Invertase Inhibitor from Maize Localizes to the Embryo Surrounding Region during Early Kernel Development

et al. 2004

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“…Pressey (18,19) showed an inhibitor was present by its purification to homogeneity and partial characterization. Invertase inhibitors have been found also in red beet, sugar beet, and sweet potato (13,20) and in maize endosperm (8). These Potatoes (Solanum tuberosum, var russet) were purchased in local supermarkets and screened for invertase and inhibitor activities.…”

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Purification and Partial Characterization of Potato (Solanum tuberosum) Invertase and Its Endogenous Proteinaceous Inhibitor

Bracho

Whitaker²

1990

Plant Physiol.

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Invertase plays an important role in the hydrolysis of sucrose in higher plants, especially in the storage organs. In potato (Solanum tuberosum) tubers, and in some other plant tissues, the enzyme seems to be controlled by interaction with an endogenous proteinaceous inhibitor. An acid invertase from potato tubers (variety russet) was purified 1560-fold to electrophoretic homogeneity by consecutive use of concanvalin A-Sepharose 4B affinity chromatography, DEAE-Sephadex A-50-120 chromatography, Sephadex G-150 chromatography, and DEAE-Sephadex A-50-120 chromatography. The enzyme contained 10.9% carbohydrate, had an apparent molecular weight of 60,000 by gel filtration, and was composed of two identical molecular weight subunits (M, 30,000). The enzyme had a Km for sucrose of 16 millimolar at pH 4.70 and was most stable and had maximum activity around pH 5. The endogenous inhibitor was purified 610-fold to homogeneity by consecutive treatment at pH 1 to 1.5 at 370C for 1 hour, (NH4)2SO4 fractionation, Sephadex G-100 chromatography, DEAESephadex G-50-120 chromatography, and hydroxylapatite chromatography. The inhibitor appears to be a single polypeptide (M, 17,000) without glyco groups. The purified inhibitor was stable over the pH range of 2 to 7 when incubated at 370C for 1 hour.Sucrose is the most abundant transportable free carbohydrate in the plant kingdom. Sucrose serves as an important reserve carbohydrate in plants, especially in such storage organs as tuber, root, and seed. During germination, sucrose is a readily degradable source of energy. In storage organs, invertase (fl-fructofuranosidase; EC 3.2.1.26) functions in the hydrolytic degradation of sucrose to glucose and fructose.Invertase was one of the first enzymes discovered; it was first isolated from yeast more than a century ago (3). The enzyme occurs widely in microbial, plant, and animal sources.

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“…Pressey (15,16) purified the inhibitor to homogeneity and partially characterized it. Invertase inhibitors have been found also in red beet, sugar beet, and sweet potato (1 1, 17) and in maize endosperm (9).…”

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Characteristics of the Inhibition of Potato (Solanum tuberosum) Invertase by an Endogenous Proteinaceous Inhibitor in Potatoes

Bracho

Whitaker²

1990

Plant Physiol.

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Effect of several parameters on inhibition of potato (Solanum tuberosum) invertase by its endogenous proteinaceous inhibitor was determined using homogeneous preparations of both proteins. The inhibitor and invertase formed an inactive complex with an observed association rate constant at pH 4.70 and 37°C of 8.82 x 102 per molar per second and a dissociation rate constant of 3.3 x 10-3 per minute. The inhibitor appeared to bind to invertase in more than one step. Initial interaction (measured by loss of invertase activity) was rapid, relatively weak, readily reversible (K, of 2 x 10-6 molar) and noncompetitive with substrate at pH 4.70. Initial interaction was probably followed by isomerization to a tighter (K, of 6.23 x 10-i molar) complex, which dissociated slowly with a half-time of 3.5 hour. Interaction between enzyme and inhibitor appeared to be of ionic character and essentially pH independent between pH 3.5 and 7.4. Schwimmer et al. (19) first reported evidence for an endogenous proteinaceous inhibitor ofinvertase in potatoes. Pressey (15,16) purified the inhibitor to homogeneity and partially characterized it. Invertase inhibitors have been found also in red beet, sugar beet, and sweet potato (1 1, 17) and in maize endosperm (9).Invertase inhibitors have been implicated in the regulation of invertase activity in several plant tissues. In potato tubers, the inhibitor may play a role in the increase of invertase activity resulting from cold treatment, wounding, or transferring of callus into liquid medium. Some aspects of the interaction between potato invertase and invertase inhibitor using crude preparations of both proteins have been reported by Ewing and McAdoo (6)

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An Invertase Inactivator in Maize Endosperm and Factors Affecting Inactivation

Cited by 57 publications

References 10 publications

An Invertase Inhibitor from Maize Localizes to the Embryo Surrounding Region during Early Kernel Development

An Invertase Inhibitor from Maize Localizes to the Embryo Surrounding Region during Early Kernel Development

Purification and Partial Characterization of Potato (Solanum tuberosum) Invertase and Its Endogenous Proteinaceous Inhibitor

Characteristics of the Inhibition of Potato (Solanum tuberosum) Invertase by an Endogenous Proteinaceous Inhibitor in Potatoes

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