Expression of Pisum sativum SAD polypeptides in production hosts and in planta: Tetrameric organization of the protein

Scherbak, Nikolai; Brosché, Mikael; Ala-Häiväla, Anneli; Strid, Hilja; Öhrfelt, Annika; Nilsson, Fred; Strid, Åke

doi:10.1016/j.pep.2008.09.004

Cited by 3 publications

(18 citation statements)

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“…The root system, unlike the stems and leaves, showed no noticeable difference in SAD protein distribution between the control tissue and tissue harvested from plants exposed to UV-B (Scherbak et al, 2009). In both cases, there was some minor immunostaining in the root cortex (data not shown).…”

Section: Detection Of Sad Protein In Pea Tissues By Immunoblot Analysmentioning

confidence: 88%

“…The highest similarities were seen with sequences from other plants (Scherbak et al, 2009): (2)-isopiperitenol dehydrogenase from Mentha species (similarity of 55%; Ringer et al, 2005), D 5 -3b-hydroxysteroid dehydrogenase (HSD; EC 1.1.1.145) from Digitalis lanata (49%; Finsterbusch et al, 1999), and secoisolariciresinol dehydrogenase from Podophyllum peltatum (46%; Xia et al, 2001). The threedimensional structure of the Podophyllum protein has been solved (Youn et al, 2005), while the Mentha protein is the polypeptide with the highest similarity to the pea SADs for which an enzymatic function is known.…”

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confidence: 88%

“…Rabbit SAD-A antiserum (which interacts with both SAD-A and SAD-C; Scherbak et al, 2009) was used in immunoblotting to determine the presence of SAD proteins in extracts of different pea tissues. This analysis showed a distribution of the SAD protein in leaves, stems, tendrils, roots, and seeds ( Fig.…”

Section: Detection Of Sad Protein In Pea Tissues By Immunoblot Analysmentioning

confidence: 99%

“…The exposure of pea plants to UV-B results in SAD mRNA accumulation in both epidermal and mesophyll cells of leaves (Kalbin et al, 2001). UV-B treatment also leads to an increase in SAD protein levels in both leaf and stem tissue but not in roots (Scherbak et al, 2009).…”

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confidence: 99%

“…SAD forms a tetramer in solution, and this is the sole oligomeric structure found under nondenaturing conditions (Scherbak et al, 2009). The pea SAD proteins are extremely similar: SAD-A and SAD-C differ by only three out of 268 amino acids .…”

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confidence: 99%

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The Pea SAD Short-Chain Dehydrogenase/Reductase: Quinone Reduction, Tissue Distribution, and Heterologous Expression

et al. 2011

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The pea (Pisum sativum) tetrameric short-chain alcohol dehydrogenase-like protein (SAD) family consists of at least three highly similar members (SAD-A, -B, and -C). According to mRNA data, environmental stimuli induce SAD expression. The aim of this study was to characterize the SAD proteins by examining their catalytic function, distribution in pea, and induction in different tissues. In enzyme activity assays using a range of potential substrates, the SAD-C enzyme was shown to reduce one-or two-ring-membered quinones lacking long hydrophobic hydrocarbon tails. Immunological assays using a specific antiserum against the protein demonstrated that different tissues and cell types contain small amounts of SAD protein that was predominantly located within epidermal or subepidermal cells and around vascular tissue. Particularly high local concentrations were observed in the protoderm of the seed cotyledonary axis. Two bow-shaped rows of cells in the ovary and the placental surface facing the ovule also exhibited considerable SAD staining. Ultraviolet-B irradiation led to increased staining in epidermal and subepidermal cells of leaves and stems. The different localization patterns of SAD suggest functions both in development and in responses to environmental stimuli. Finally, the pea SAD-C promoter was shown to confer heterologous wound-induced expression in Arabidopsis (Arabidopsis thaliana), which confirmed that the inducibility of its expression is regulated at the transcriptional level.

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Section: Detection Of Sad Protein In Pea Tissues By Immunoblot Analysmentioning

confidence: 88%

mentioning

confidence: 88%

Section: Detection Of Sad Protein In Pea Tissues By Immunoblot Analysmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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The Pea SAD Short-Chain Dehydrogenase/Reductase: Quinone Reduction, Tissue Distribution, and Heterologous Expression

et al. 2011

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Genetic Adjustment to Changing Climates: Pea

Coyne¹,

McGee²,

Redden³

et al. 2011

Crop Adaptation to Climate Change

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The RST and PARP-like domain containing SRO protein family: analysis of protein structure, function and conservation in land plants

et al. 2010

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BackgroundThe SROs (SIMILAR TO RCD-ONE) are a group of plant-specific proteins which have important functions in stress adaptation and development. They contain the catalytic core of the poly(ADP-ribose) polymerase (PARP) domain and a C-terminal RST (RCD-SRO-TAF4) domain. In addition to these domains, several, but not all, SROs contain an N-terminal WWE domain.ResultsSROs are present in all analyzed land plants and sequence analysis differentiates between two structurally distinct groups; cryptogams and monocots possess only group I SROs whereas eudicots also contain group II. Group I SROs possess an N-terminal WWE domain (PS50918) but the WWE domain is lacking in group II SROs. Group I domain structure is widely represented in organisms as distant as humans (for example, HsPARP11). We propose a unified nomenclature for the SRO family. The SROs are able to interact with transcription factors through the C-terminal RST domain but themselves are generally not regulated at the transcriptional level. The most conserved feature of the SROs is the catalytic core of the poly(ADP-ribose) polymerase (PS51059) domain. However, bioinformatic analysis of the SRO PARP domain fold-structure and biochemical assays of AtRCD1 suggested that SROs do not possess ADP-ribosyl transferase activity.ConclusionsThe SROs are a highly conserved family of plant specific proteins. Sequence analysis of the RST domain implicates a highly preserved protein structure in that region. This might have implications for functional conservation. We suggest that, despite the presence of the catalytic core of the PARP domain, the SROs do not possess ADP-ribosyl transferase activity. Nevertheless, the function of SROs is critical for plants and might be related to transcription factor regulation and complex formation.

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Expression of Pisum sativum SAD polypeptides in production hosts and in planta: Tetrameric organization of the protein

Cited by 3 publications

References 34 publications

The Pea SAD Short-Chain Dehydrogenase/Reductase: Quinone Reduction, Tissue Distribution, and Heterologous Expression

The Pea SAD Short-Chain Dehydrogenase/Reductase: Quinone Reduction, Tissue Distribution, and Heterologous Expression

Genetic Adjustment to Changing Climates: Pea

The RST and PARP-like domain containing SRO protein family: analysis of protein structure, function and conservation in land plants

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