Stable expression of maize auxin‐binding protein in insect cell lines

Henderson, Jeffrey; Atkinson, Allan E.; Lazarus, Colin M.; Hawes, Chris; Napier, Richard; Macdonald, Heather; King, Linda A.

doi:10.1016/0014-5793(95)00922-v

Cited by 11 publications

(1 citation statement)

References 10 publications

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“…Moreover, it should be noted that in the purification process of soybean oil, a byproduct named “gum” is a material enriched in phospholipids (about 65% of dry weight), which is usually used in animal’s food production or, after drying, it is sold as soybean lecithin . The hydrolytic products obtained by the action of sPLA 2 over soybean lecithin, the lysophospholipids (lysoderivatives), are widely used as emulsifiers (Henderson et al, 1995; Dashiell, 2001).…”

Section: Potential Industrial Application and Perspectivesmentioning

confidence: 99%

Secretory Phospholipases A2 in Plants

Mariani

Fidelio

2019

Front. Plant Sci.

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Secreted phospholipases (sPLA 2 s) in plants are a growing group of enzymes that catalyze the hydrolysis of sn-2 glycerophospholipids to lysophospholipids and free fatty acids. Until today, around only 20 sPLA 2 s were reported from plants. This review discusses the newly acquired information on plant sPLA 2 s including molecular, biochemical, catalytic, and functional aspects. The comparative analysis also includes phylogenetic, evolutionary, and tridimensional structure. The observations with emphasis in Glycine max sPLA 2 are compared with the available data reported for all plants sPLA 2 s and with those described for animals (mainly from pancreatic juice and venoms sources).

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Section: Potential Industrial Application and Perspectivesmentioning

confidence: 99%

Secretory Phospholipases A2 in Plants

Mariani

Fidelio

2019

Front. Plant Sci.

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Retention of maize auxin-binding protein in the endoplasmic reticulum: quantifying escape and the role of auxin

Henderson

Bauly²,

Ashford

et al. 1997

Planta

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The localisation of maize (Zea mays L.) auxin-binding protein (ABP1) has been studied using a variety of techniques. At the whole-tissue level, tissue printing indicated that ABP1 is expressed to similar levels in all cells of the maize coleoptile and in the enclosed leaf roll. Within cells, the signals from immunofluorescence and immunogold labelling of ultrathin sections both indicated that ABP1 is confined to the endoplasmic reticulum (ER), none being detected in either Golgi apparatus or cell wall. This distribution is consistent with targeting motifs in its sequence. These observations are discussed with reference to the various reports which place a population of ABP1 on the outer face of the plasma membrane, including those suggesting that it is necessary on the cell surface for rapid, auxin-mediated protoplast hyperpolarisation. We have tested the ER, namely that auxin binding induces a conformational change in ABP1 leading to concealment of the KDEL retention motif. Using double-label immunofluorescence the characteristic auxin-induced rise in Golgi-apparatus signal was found, yet no change in the distribution of the ABP1 signal was detected. Maize suspension cultures were used to assay for auxin-promoted secretions of ABP1 into the medium, but secretion was below the limit of detection. This can be ascribed at least partly to the very active acidification of the medium by these cells and the instability of ABP 1 in solution below pH 5.0. In the insect-baculovirus expression system, in which cell cultures maintain pH 6.2, a small amount of ABP1 secretion, less than 1% of the total, was detected under all conditions, Insect cells were shown to take up auxin and no inactivation of added auxin was detected, but auxin did not affect the level of ABP1 in the medium. Consequently, no evidence was found to support the model for auxin promotion of ABP1 secretion. Finally, quantitative glycan analysis was used to determine what proportion of ABP1 might reach the plasma membrane in maize coleoptile tissue. The results suggest that less than 15% of ABP1 ever escapes from the ER as far as the cis-Golgi and less than 2% passes further through the secretory pathway. Such leakage rates probably do not require a specialised mechanism allowing ABP1 past the KDEL retrieval pathway, but we are not able to rule out the possibility that some ABP1 is carried through associated with other proteins. The data are consistent with the presence of ABP1 both on the plasma membrane and in the ER. The relative sizes of the two pools explain the results obtained with immunofluorescence and immunogold labelling and illustrate the high efficiency of ER retention in plants.

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Characterization of auxin-binding protein 1 from tobacco: content, localization and auxin-binding activity

Shimomura

Watanabe

Ichikawa

1999

Planta

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There is evidence that auxin-binding protein 1 (ABP1) is an auxin receptor on the plasma membrane. Maize (Zea mays L.) possesses a high level of auxin-binding activity due to ABP1, but no other plant source has been shown to possess such an activity. We have analyzed the ABP1 content of tobacco (Nicotiana tabacum L.) to examine whether or not the ABP1 content of maize is exceptionally high among plants. The ABP1 content of tobacco leaves was shown by quantitative immunoblot analysis to be between 0.7 and 1.2 microg ABP1 per gram of fresh leaf. This value is comparable to the reported value in maize shoots, indicating that ABP1 is present at a similar level in both monocot and dicot plants. The ABP1 content of tobacco leaves was increased up to 20-fold by expression of a recombinant ABP1 gene, and decreased to half of the original value by expression of the antisense gene. Although ABP1 was found mainly in the endoplasmic reticulum fraction, a secreted protein showing a molecular size and epitopes similar to intracellular ABP1 was also detected in the culture medium of tobacco leaf disks. The secretion of this protein was dependent on the expression level of the ABP1 gene.

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Stable expression of maize auxin‐binding protein in insect cell lines

Cited by 11 publications

References 10 publications

Secretory Phospholipases A2 in Plants

Secretory Phospholipases A2 in Plants

Retention of maize auxin-binding protein in the endoplasmic reticulum: quantifying escape and the role of auxin

Characterization of auxin-binding protein 1 from tobacco: content, localization and auxin-binding activity

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