Genotypic variation in sulphur assimilation and metabolism of onion (Allium cepa L.). II: Characterisation of ATP sulphurylase activity

Handle URI:
http://hdl.handle.net/10754/561785
Title:
Genotypic variation in sulphur assimilation and metabolism of onion (Allium cepa L.). II: Characterisation of ATP sulphurylase activity
Authors:
Thomas, Ludivine; Leung, Susanna; Cumming, Mathew; Shaw, Martin L.; Albert, Nick W.; McCallum, John A.; McManus, Michael T.
Abstract:
To investigate the regulation of sulphur (S)-assimilation in onion further at the biochemical level, the pungent cultivar W202A and the milder cultivar Texas Grano 438 PVP (TG) have been grown in S-sufficient (S +; 4 meq S -1) or S-deficient (S -; 0.1 meq S -1) growth conditions, and tissues excised at the seedling stage (pre-bulbing; ca. 10-weeks-old) and at the mature stage (bulbing; ca. 16-weeks-old). S-supply negatively influenced adenosine-5′-phosphosulphate (APS) reductase (APR) enzyme activity in both cultivars at bulbing only, and a higher abundance of APR was observed in both cultivars at bulbing in response to low S-supply. In contrast, S-supply significantly influenced ATP sulphurylase (ATPS) activity in leaf tissues of W202A only, and only at bulbing, while an increase in abundance in response to high S-supply was observed for both cultivars at bulbing. To investigate the regulation of the ATPS enzyme activity and accumulation further, activity was shown to decrease significantly in roots at bulbing in the S-deficient treatment in both cultivars, a difference that was only supported by western analyses in W202A. Phylogenetic analysis revealed that AcATPS1 groups in a broad monocot clade with the closest sequences identified in Sorghum bicolour, Zea mays and Oryza sativa, but with some support for a divergence of AcATPS1. Detection of ATPS in leaf extracts after two dimensional gel electrophoresis (2-DE) revealed that the protein may undergo post-translational modification with a differential pattern of ATPS accumulation detected in both cultivars over the developmental progression from the seedling to the bulbing stage. Treatment of leaf extracts of W202A to dephosphorylate proteins resulted in the loss of immuno-recognised ATPS spots after 2-DE separation, although enzyme activity was not influenced. These results are discussed in terms of the tiers of control that operate at the biochemical level in the reductive S-assimilation pathway in a S-accumulating species particularly during the high-S-demanding bulbing stage. © 2011 Elsevier Ltd. All rights reserved.
KAUST Department:
Computational Bioscience Research Center (CBRC); Core Labs
Publisher:
Elsevier BV
Journal:
Phytochemistry
Issue Date:
Jun-2011
DOI:
10.1016/j.phytochem.2011.03.001
Type:
Article
ISSN:
00319422
Appears in Collections:
Articles; Computational Bioscience Research Center (CBRC)

Full metadata record

DC FieldValue Language
dc.contributor.authorThomas, Ludivineen
dc.contributor.authorLeung, Susannaen
dc.contributor.authorCumming, Mathewen
dc.contributor.authorShaw, Martin L.en
dc.contributor.authorAlbert, Nick W.en
dc.contributor.authorMcCallum, John A.en
dc.contributor.authorMcManus, Michael T.en
dc.date.accessioned2015-08-03T09:04:34Zen
dc.date.available2015-08-03T09:04:34Zen
dc.date.issued2011-06en
dc.identifier.issn00319422en
dc.identifier.doi10.1016/j.phytochem.2011.03.001en
dc.identifier.urihttp://hdl.handle.net/10754/561785en
dc.description.abstractTo investigate the regulation of sulphur (S)-assimilation in onion further at the biochemical level, the pungent cultivar W202A and the milder cultivar Texas Grano 438 PVP (TG) have been grown in S-sufficient (S +; 4 meq S -1) or S-deficient (S -; 0.1 meq S -1) growth conditions, and tissues excised at the seedling stage (pre-bulbing; ca. 10-weeks-old) and at the mature stage (bulbing; ca. 16-weeks-old). S-supply negatively influenced adenosine-5′-phosphosulphate (APS) reductase (APR) enzyme activity in both cultivars at bulbing only, and a higher abundance of APR was observed in both cultivars at bulbing in response to low S-supply. In contrast, S-supply significantly influenced ATP sulphurylase (ATPS) activity in leaf tissues of W202A only, and only at bulbing, while an increase in abundance in response to high S-supply was observed for both cultivars at bulbing. To investigate the regulation of the ATPS enzyme activity and accumulation further, activity was shown to decrease significantly in roots at bulbing in the S-deficient treatment in both cultivars, a difference that was only supported by western analyses in W202A. Phylogenetic analysis revealed that AcATPS1 groups in a broad monocot clade with the closest sequences identified in Sorghum bicolour, Zea mays and Oryza sativa, but with some support for a divergence of AcATPS1. Detection of ATPS in leaf extracts after two dimensional gel electrophoresis (2-DE) revealed that the protein may undergo post-translational modification with a differential pattern of ATPS accumulation detected in both cultivars over the developmental progression from the seedling to the bulbing stage. Treatment of leaf extracts of W202A to dephosphorylate proteins resulted in the loss of immuno-recognised ATPS spots after 2-DE separation, although enzyme activity was not influenced. These results are discussed in terms of the tiers of control that operate at the biochemical level in the reductive S-assimilation pathway in a S-accumulating species particularly during the high-S-demanding bulbing stage. © 2011 Elsevier Ltd. All rights reserved.en
dc.publisherElsevier BVen
dc.subjectAllium cepa L.en
dc.subjectAPR reductaseen
dc.subjectATP sulphurylaseen
dc.subjectChloroplastsen
dc.subjectEnzyme activityen
dc.subjectSulphur assimilationen
dc.titleGenotypic variation in sulphur assimilation and metabolism of onion (Allium cepa L.). II: Characterisation of ATP sulphurylase activityen
dc.typeArticleen
dc.contributor.departmentComputational Bioscience Research Center (CBRC)en
dc.contributor.departmentCore Labsen
dc.identifier.journalPhytochemistryen
dc.contributor.institutionInstitute of Molecular BioSciences, Massey University, Private Bag 11222, Palmerston North, New Zealanden
dc.contributor.institutionNew Zealand Institute for Plant and Food Research Ltd., Private Bag 4704, Christchurch, New Zealanden
kaust.authorThomas, Ludivineen
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