Hardening of clerodendrum to chilling: chemical treatments and growth at low temperatures

Tamari, Guy; Tandler, J.; Borochov, Amihud

doi:10.1016/0304-4238(92)90126-w

Cited by 7 publications

(7 citation statements)

References 15 publications

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“…, 2006). Moreover, reducing the GA level in Clerodendrum speciosum enhanced resistance to low‐temperature stress (Tamari et al. , 1992).…”

Section: Discussionmentioning

confidence: 99%

“…For example, the Arabidopsis GA-deficient mutant ga1-3 is relatively resistant to salt stress (Achard et al, 2006). Moreover, reducing the GA level in Clerodendrum speciosum enhanced resistance to low-temperature stress (Tamari et al, 1992). Both low temperature and salt are known to induce oxidative stress (Allen and Ort, 2001;Avsian-Kretchmer et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

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The gibberellin‐induced, cysteine‐rich protein GIP2 from Petunia hybrida exhibits in planta antioxidant activity

et al. 2006

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SummaryNumerous GAST-like genes have been identified in various plant species. All code for small proteins with a conserved C-terminal region in which 12 cysteines are located in exactly the same positions. We have previously identified five gibberellin (GA)-induced GAST1-like genes in petunia, GIP1-5. GIP2 is expressed in elongating zones, and its suppression in transgenic petunia plants inhibits stem elongation, suggesting a role for the protein in GA-induced cell growth. However, nothing is known about the biochemical activity of GIP2 or any other GAST-like protein. As all contain putative catalytic disulfide bonds (putative redox-active cysteines), we speculated that they might be involved in redox regulation. Expression analysis of GIP2, GIP4 and GIP5 revealed that they are induced by H 2 O 2 . To study whether GIP2 modulates H 2 O 2 levels, we generated transgenic petunia plants expressing GIP2 under the regulation of the ubiquitous CaMV 35S promoter. The transgene reduced H 2 O 2 levels in leaves following wounding. It also reduced the levels of H 2 O 2 in guard cells following osmotic stress and ABA treatments, leading to the suppression of stomatal closure. In addition, the transgene promoted stem and corolla elongation. As reactive oxygen species (ROS) are involved in cell elongation, we suggest that GIP2 affects growth by regulating the levels of ROS. As all known GAST-like proteins contain putative redox-active cysteines, they may all act as antioxidants.

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“…, 2006). Moreover, reducing the GA level in Clerodendrum speciosum enhanced resistance to low‐temperature stress (Tamari et al. , 1992).…”

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

The gibberellin‐induced, cysteine‐rich protein GIP2 from Petunia hybrida exhibits in planta antioxidant activity

et al. 2006

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“…This consistent trend confirms the sensitivity of roses to LTI. Cell membranes in low temperature-or chilling-sensitive cut flowers Effects of storage temperature and ABA on cut roses undergo alterations in their structure which lead to electrolyte leakage (Borochov and Shahar, 1989;Tamari et al, 1992). The magnitude of the increase in electrolyte leakage at 1°C was greater in 'Akito' than in 'First Red' roses, indicating possible genotypic differences in the degree of sensitivity to LTI (Figure 3).…”

Section: Effects Of Storage Temperature On Vase-life Parametersmentioning

confidence: 93%

Effects of storage temperature and abscisic acid treatment on the vase-life of cut ‘First Red’ and ‘Akito’ roses

Pompodakis

Terry

Joyce

et al. 2010

The Journal of Horticultural Science and Biotechnology

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Abscisic acid (ABA) treatment can confer chilling tolerance upon certain plant tissues that suffer injury at low temperatures. The present study investigated the efficacy of two post-harvest ABA treatments in suppressing low temperature injury (LTI) in cut rose (Rosa hybrida L.) flowers stored at 1°C or 5°C. A shortened vase-life was recorded for roses stored at 5°C compared to untreated roses and those stored at 1°C. Storage at 1°C significantly (P ≤ 0.01) increased electrolyte leakage in 'Akito' roses compared to roses stored at 5°C, or to untreated roses. Storage of 'First Red' and 'Akito' roses at 1°C or 5°C significantly (P ≤ 0.01) increased the malondialdehyde (MDA) contents of petal and leaf tissues. The highest MDA contents were recorded in roses stored at 1°C. ABA at 10 µM as a spray, or at 0.1 M as a pulse treatment, did not affect the MDA contents of either leaves or petals. When averaged over the two storage temperature treatments, the ABA content was highest in roses pulse-treated with 0.1 M ABA, followed by those sprayed with 10 µM ABA, then by untreated (control) roses. However, this increase did not have any apparent effect on the longevity or senescence of the cut roses. Moreover, this trend was inconsistent across all storage treatments. Pulsing with 0.1 M ABA or spraying with 10 µM ABA before storage did not significantly (P > 0.05) affect vase-life. However, pulsing 'Akito' roses with 0.1 M ABA before storage tended to reduce the level of electrolyte leakage from leaves.

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“…With clerodendrum (Clerodendrum speciosum), as with most other chilling-sensitive plants, the first visual symptom of chilling injury is leaf wilting. Wilting is accompanied by a massive leakage of cellular electrolytes (10), indicating that there are chillinginduced changes in the cell membranes. Indeed, we have reported recently on a decrease in the content of leaf membrane phospholipids and proteins following a transient exposure of clerodendrum plants to chilling (10).…”

Section: Membrane Preparationmentioning

confidence: 99%

“…Plants were grown at 27/180C (day/night) under LD conditions as described before (10). Chilling was induced by exposing the plants to 30C for 48 h in a temperature-controlled chamber.…”

mentioning

confidence: 99%

Ubiquitin Conjugation to Protein Increases following Chilling of Clerodendrum Leaves

Gindin¹,

Borochov²

1992

Plant Physiol.

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The protein content of clerodendrum (Clerodendrum speciosum) leaves declines following chilling (48 h, 3°C). Using western and dot blots and fluorescence immunoassays, we found that isolated leaf proteins had more conjugated ubiquitin following chilling. In contrast, the amount of free ubiquitin declined by almost 90% after chilling. The increase in ubiquitin conjugation was greater in the membrane fraction than in the soluble fraction.Plants were grown at 27/180C (day/night) under LD conditions as described before (10). Chilling was induced by exposing the plants to 30C for 48 h in a temperature-controlled chamber. Analyses of fully grown leaves were done within 1 h after the end of the treatments. Membrane PreparationChilling injury occurs in many tropical and subtropical plants following exposure Microsomal membranes were isolated from the leaves in the presence of 2 mm DTT and 2 mm PMSF using differential centrifugation as described previously (7). The membrane pellets were resuspended in 20 mm Tris-HCl at pH 7.4. To get a free ubiquitin fraction, the obtained supematant was filtered through a YM10 membrane using an ultrafiltration cell (Amicon); after this was done, the effluent was free of proteins larger than 10,000 kD. During all of the isolation steps, the temperature was kept at 0 to 40C. Immediately following isolation, protein content was determined according to Bradford (2), and the various analyses were conducted. FIA2Quantitative analysis of the ubiquitin was conducted by FIA according to a manufacturer's (Sigma) protocol: Ubiquitin-fluorescein conjugate (100 ,uL) at 20.4 pmol/mL (Sigma U-5540) was added to all test tubes except the blanks. A sample (100 ,uL of a 1 mg protein/mL solution) to be tested was added to all tubes. Finally, 100 yL of rabbit anti-ubiquitin IgG (Sigma U-5379) was added to all samples. The samples were mixed by vortexing and incubated for 60 min at room temperature in the dark. Then, 1 mL of immunoprecipitation reagent (goat anti-rabbit IgG in 0.1 M PBS) was added to each test tube, and the samples were centrifuged at 2000g for 15 min at 40C. The supematants were aspirated and discarded, and the pellets were resuspended in 3 mL of 0.1 N NaOH in 2% SDS. The samples were excited at 494 nm and the fluorescence was measured at 516 nm using a spectrofluorimeter (SLM model 4600). A decrease in the immunoprecipitated fluorescein-labeled ubiquitin resulted in a decrease in the fluorescence intensity and indicated a higher level of ubiquitin in the tested sample. The amount of the ubiquitin in the samples was calculated according to a calibration curve, which was prepared with purified ubiquitin (Sigma) (Fig. 1).

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Hardening of clerodendrum to chilling: chemical treatments and growth at low temperatures

Cited by 7 publications

References 15 publications

The gibberellin‐induced, cysteine‐rich protein GIP2 from Petunia hybrida exhibits in planta antioxidant activity

The gibberellin‐induced, cysteine‐rich protein GIP2 from Petunia hybrida exhibits in planta antioxidant activity

Effects of storage temperature and abscisic acid treatment on the vase-life of cut ‘First Red’ and ‘Akito’ roses

Ubiquitin Conjugation to Protein Increases following Chilling of Clerodendrum Leaves

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