Nitric oxide and salicylic acid signaling in plant defense

Klessig, Daniel F.; Durner, Jörg; Noad, Rob; Navarre, Duroy A.; Wendehenne, David; Kumar, Dhirendra; Zhou, Jun; Shah, Jyoti; Zhang, Shuqun; Kachroo, Pradeep; Trifa, Youssef; Pontier, Dominique; Lam, Eric; Silva, Herman

doi:10.1073/pnas.97.16.8849

Cited by 653 publications

(423 citation statements)

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“…NOS activities are present in plants and lower eukaryotes (1)(2)(3)(4)(5). Their primary structures and activities are strikingly similar to the mammalian NOSs, suggesting that NO has been important throughout evolution.…”

mentioning

confidence: 91%

Cloning, expression, and characterization of a nitric oxide synthase protein from Deinococcus radiodurans

Adak

Bilwes

Panda

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

122

139

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We cloned, expressed, and characterized a hemeprotein from Deinococcus radiodurans (D. radiodurans NO synthase, deiNOS) whose sequence is 34% identical to the oxygenase domain of mammalian NO synthases (NOSoxys). deiNOS was dimeric, bound substrate Arg and cofactor tetrahydrobiopterin, and had a normal heme environment, despite its missing N-terminal structures that in NOSoxy bind Zn 2؉ and tetrahydrobiopterin and help form an active dimer. The deiNOS heme accepted electrons from a mammalian NOS reductase and generated NO at rates that met or exceeded NOSoxy. Activity required bound tetrahydrobiopterin or tetrahydrofolate and was linked to formation and disappearance of a typical heme-dioxy catalytic intermediate. Thus, bacterial NOS-like proteins are surprisingly similar to mammalian NOSs and broaden our perspective of NO biochemistry and function.G enes coding for NO synthases (NOSs, EC 4.14.23) are present throughout the plant and animal kingdom. NOS activities are present in plants and lower eukaryotes (1-5). Their primary structures and activities are strikingly similar to the mammalian NOSs, suggesting that NO has been important throughout evolution. All eukaryotic NOSs catalyze the NADPH-and O 2 -dependent oxidation of L-arginine (Arg) to citrulline and NO, with N-hydroxy-L-arginine (NOHA) formed as an enzyme-bound intermediate (6). Structurally, all animal NOSs are bi-domain proteins containing an N-terminal oxygenase domain (NOSoxy) that binds protoporphyrin IX (heme), 6R-tetrahydrobiopterin (H 4 B), and Arg and is linked to a C-terminal f lavoprotein domain (NOS reductase domain, NOSred) by a central calmodulin (CaM) binding sequence (7,8). NOSred bears strong sequence and functional similarity to NADPH-cytochrome P450 reductase and related electron transfer flavoproteins (9, 10), and function to transfer NADPHderived electrons to the ferric heme for O 2 activation during NO synthesis. In contrast, NOSoxy and cytochromes P450 have completely different primary, secondary, and tertiary structures, even though both enzyme families use a thiolate-ligated heme for O 2 activation (11, 12). Moreover, unlike P450s, NOSoxy must dimerize to become active (13,14). Dimerization produces functional binding sites for Arg and H 4 B and sequesters the heme catalytic center from solvent. These distinguishing features imply that NOSs evolved separately from other heme-thiolate enzymes and can so provide unique perspectives on their structure-function relationships.Although oxidative (nitrification) or reductive (denitrification) pathways for prokaryote NO biosynthesis are well established (15), there have been few reports on NOS-like proteins in bacteria (16,17). To date no prokaryotic NOS proteins have been completely sequenced, purified, or cloned. However, some have been shown to have nitrite-forming activity that depended on Arg, NADPH, and H 4 B. More recent genome sequencing of Bacillus subtilis, Deinococcus radiodurans, and other bacteria (18)(19)(20) confirm that a subset contain ORFs that code for proteins homo...

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mentioning

confidence: 91%

Cloning, expression, and characterization of a nitric oxide synthase protein from Deinococcus radiodurans

Adak

Bilwes

Panda

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

122

139

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“…Salicylic acid is probably the most well-characterized signaling molecule in plant defense reactions (Klessig et al, 2000), but signal transduction pathways involving methyl jasmonate and ethylene have also been characterized (Reymond and Farmer, 1998). On the other hand, auxin has been shown to activate some defense-related genes through the as-1 element, which also confers inducibility by salicylic acid (Strompen et al, 1988;Xiang et al, 1996).…”

Section: Retrotransposons As Models To Analyze Stressassociated Exprementioning

confidence: 99%

Three Tnt1 Subfamilies Show Different Stress-Associated Patterns of Expression in Tobacco. Consequences for Retrotransposon Control and Evolution in Plants

et al. 2001

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The genomes of most Nicotiana species contain three different subfamilies of the Tnt1 retrotransposon, which differ completely in their U3 sequence, whereas the rest of the sequence is relatively constant. The results presented here show that all three Tnt1 subfamilies are expressed in tobacco (Nicotiana tabacum) and that the U3 sequence variability correlates with differences in the pattern of expression of the Tnt1 elements. Each of the three Tnt1 subfamilies is induced by stress, but their promoters have a different response to different stress-associated signaling molecules. The Tnt1A subfamily is particularly strongly induced by elicitors and methyl jasmonate, whereas expression of the Tnt1C subfamily is more sensitive to salicylic acid and auxins. The direct relationship between U3 sequence variability and differences in the stress-associated expression of the Tnt1 elements present in a single host species gives support to our model that postulates that retrotransposons have adapted to their host genomes through the evolution of highly regulated promoters that mimic those of the stress-induced plant genes. Moreover, here we show that the analysis of the transcriptional control of a retrotransposon population such as Tnt1 provides new insights into the study of the complex and still poorly understood network of defense-and stress-induced plant signal transduction pathways.

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“…NO synthesis was blocked with 5 mM N-methyl-L-arginine (L-NMMA), a nitrogen oxide synthase (NOS) inhibitor [8]. 1186 T. S. Gechev, I.…”

Section: Inhibition Of Ethylene Production and No Synthesismentioning

confidence: 99%

An extensive microarray analysis of AAL-toxin-induced cell death in Arabidopsis thaliana brings new insights into the complexity of programmed cell death in plants

Gechev

Gadjev

Hille

2004

Cellular and Molecular Life Sciences (CMLS)

129

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An extensive microarray analysis of AAL-toxin-induced cell death in Arabidopsis thaliana brings new insights into the complexity of programmed cell death in plants Gechev, T.S.; Gadjev, I.Z.; Hille, J. Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim. Abstract. A T-DNA knockout of the Arabidopsis homologue of the tomato disease resistance gene Asc was obtained. The asc gene renders plants sensitive to programmed cell death (PCD) triggered by the fungal AAL toxin. To obtain more insights into the nature of AALtoxin-induced cell death and to identify genes of potential importance for PCD, we carried out transcription profiling of AAL-toxin-induced cell death in this knockout with an oligonucleotide array representing 21,500 Arabidopsis genes. Genes responsive to reactive oxygen species (ROS) and ethylene were among the earliest to be upregulated, suggesting that an oxidative burst and production of ethylene played a role in the activation of the cell death. This notion was corroborated by induction of several genes encoding ROS-generating proteins, including a respiratory burst oxidase and germin oxalate oxi- CMLS, Cell. Mol. Life Sci. 61 (2004) 1185 -1197 1420-682X/04/101185-13 DOI 10.1007/s00018-004-4067-2 © Birkhäuser Verlag, Basel, 2004 CMLS Cellular and Molecular Life Sciences dase. Cytochemical studies confirmed the oxidative burst and, in addition, showed synthesis of callose, a feature of the hypersensitive response. A diverse group of transcription factors was also induced. These events were followed by repression of most of the auxin-regulated genes known to be involved in growth and developmental responses. All photosynthesis-related genes were repressed. Blocking the synthesis of ethylene or NO significantly compromised cell death. In addition, we identified a heterogeneous group of early-induced genes, some of them never before associated with PCD. The group of earlyinduced genes included a number of proteases that were previously implicated in developmentally regulated types of PCD, suggesting a more principal role for these proteases in the PCD process. These findings provide new insights into the molecular mechanisms of plant PCD.

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Nitric oxide and salicylic acid signaling in plant defense

Abstract: MAP kinases ͉ Ca ϩ2 ͉ cADP ribose ͉ cGMP ͉ disease resistance

Cited by 653 publications

References 88 publications

Cloning, expression, and characterization of a nitric oxide synthase protein from Deinococcus radiodurans

Cloning, expression, and characterization of a nitric oxide synthase protein from Deinococcus radiodurans

Three Tnt1 Subfamilies Show Different Stress-Associated Patterns of Expression in Tobacco. Consequences for Retrotransposon Control and Evolution in Plants

An extensive microarray analysis of AAL-toxin-induced cell death in Arabidopsis thaliana brings new insights into the complexity of programmed cell death in plants

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