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At least 109 records · Page 6Linked to original sources
PubMed2006

Roles of salicylic acid-responsive cis-acting elements and W-boxes in salicylic acid induction of VCH3 promoter in transgenic tobaccos.

A salicylic acid (SA)-inducible VCH3 promoter was recently identified from grapevine (Vitis amurensis) that contains two inverse SA-responsive cis-acting elements and four W-boxes. To further demonstrate the roles of these elements, four fragments with lengths from -1187, -892, -589, -276 to +7 bp were fused with the b-glucuronidase (GUS) reporter gene and transferred to Nicotiana tobacum, together with another four VCH3 promoter fragments with mutation in the two inverse SA-responsive elements. The functions of each promoter fragment were examined by analysis of GUS activity in the transgenic tobacco root treated with SA. Enhanced GUS activity was shown in the roots of transgenic tobaccos with the VCH3 (-1187)-GUS construct containing two SA-responsive cis-acting elements and four W-boxes. However, GUS activity directed by the VCH3 (-892)-GUS construct, containing one SA cis-acting element and four W-boxes, was reduced by up to 35% compared with that in tobaccos transformed with the VCH3 (-1187)-GUS construct, indicating that the SA cis-acting element plays an important role in SA induction of the VCH3 promoter. Neither the m2VCH3 (-1187)-GUS nor the mVCH3 (-892)-GUS construct, with mutation on the SA-responsive elements, abolished the expression of GUS activity, demonstrating that the W-boxes in the VCH3 promoter are also involved in SA induction. Histochemical analysis of GUS activity directed by each of the eight VCH3 promoter fragments showed that GUS was expressed specifically in vascular tissue. It was concluded that both the SA-responsive cis-acting elements and the W-boxes are important for the SA induction of the VCH3 promoter. This promoter might have a potential use in plant genetic engineering.

Gene Deletion↗
PubMed2001

Salicylic acid response in rice: influence of salicylic acid on H(2)O(2) accumulation and oxidative stress.

We have studied the accumulation of hydrogen peroxide in rice leaves in response to salicylic acid (SA) treatment. H(2)O(2) accumulation was localized in the veins. While the activity of the H(2)O(2) degrading enzyme peroxidase was inhibited in response to SA, superoxide dismutase activity, which generates H(2)O(2), did not show any change. An increase in the activity of glutathione reductase, a peroxide degrading enzyme, was observed upon SA treatment, similar to the response reported by accumulation of active oxygen species. In rice leaves transformed with CaMV-GUS fusions, we found that SA treatment induced transcriptional activation through as-1 element. As-1 has been implicated in protective mechanisms that operate during some types of oxidative stress and the hypersensitive response (HR). Expression of rice pathogenesis-related protein 5 (PR5), one of the PR genes associated with systemic acquired resistance, was induced by SA. This induction seems to be independent of the H(2)O(2) accumulation induced by SA. Inoculation of rice leaves with the rice blast fungus, Magneporthe grisea, also led to the accumulation of H(2)O(2) in the veins, suggesting the presence of common signals between SA and pathogen responses. Thus SA application seems to induce oxidative stress in rice through H(2)O(2); a signal molecule implicated in biotic and abiotic stress responses.

Journal Article↗
PubMed2002

Heterometallic CeIII-FeIII-salicylate networks: models for corrosion mitigation of steel surfaces by the 'green' inhibitor, Ce(salicylate)3.

The syntheses and structures of the novel Ce-Fe bimetallic complexes [[Fe(sal)2(bpy)]2Ce(NO3)(H2O)3].EtOH and [[Fe(sal)2(bpy)]4Ce2(H2O)11][salH]2.EtOH.3H2O (salH2 = salicylic acid) suggest Fe(3+)-sal2- units and Ce-OC(R)O-Fe bridging contribute to the formation of corrosion inhibitive layers on steel surfaces exposed to [Ce(salH)3(H2O)].

Journal Article↗
PubMed1994

A Salicylic Acid-Binding Activity and a Salicylic Acid-Inhibitable Catalase Activity Are Present in a Variety of Plant Species.

Recently, it has been demonstrated that the salicylic acid (SA)-binding protein (SABP) from tobacco (Nicotiana tabacum) is a SA-inhibitable catalase (Z. Chen, H. Silva, D.F. Klessig [1993] Science 262: 1883-1886). Here we report the presence of SABP and SA-inhibitable catalase activity in Arabidopsis, tomato, and cucumber. The cucumber SABP has properties similar to the tobacco SABP, including binding affinity and specificity for SA.

Journal Article↗
PubMed1997

Differential Accumulation of Salicylic Acid and Salicylic Acid-Sensitive Catalase in Different Rice Tissues.

We previously proposed that salicylic acid (SA)-sensitive catalases serve as biological targets of SA in plant defense responses. To further examine the role of SA-sensitive catalases, we have analyzed the relationship between SA levels and SA sensitivity of catalases in different rice (Oryza sativa) tissues. We show here that, whereas rice shoots contain extremely high levels of free SA, as previously reported (I. Raskin, H. Skubatz, W. Tang, B.J.D. Meeuse [1990] Ann Bot 66: 369-373; P. Silverman, M. Seskar, D. Kanter, P. Schweizer, J.-P. Metraux, I. Raskin [1995] Plant Physiol 108: 633-639), rice roots and cell-suspension cultures have very low SA levels. Catalases from different rice tissues also exhibit differences in sensitivity to SA. Catalase from rice shoots is insensitive to SA, but roots and cell-suspension cultures contain SA-sensitive catalase. The difference in SA sensitivity of catalases from these different tissues correlates with the tissue-specific expression of two catalase genes, CatA and CatB, which encode highly distinctive catalase proteins. CatA, which encodes a catalase with relatively low sequence homology to the tobacco SA-sensitive catalases, is expressed at high levels exclusively in the shoots. On the other hand, in roots and cell-suspension cultures, with northern analysis we detected expression of only the CatB gene, which encodes a catalase with higher sequence homology to tobacco catalases. The role of catalases in mediating some of the SA-induced responses is discussed in light of these results and the recently defined mechanisms of catalase inhibition by SA.

Journal Article↗