Bax-induced cell death in tobacco is similar to the hypersensitive response

Lacomme, Christophe; Cruz, Simon Santa

doi:10.1073/pnas.96.14.7956

Cited by 399 publications

(326 citation statements)

References 50 publications

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“…78 Although informatics has failed to identify BAX, BCL2, and BCLX L sequence homologs in either the Arabidopsis or yeast (Saccharomyces cerevisiae) genomes, there is evidence that the basic regulatory mechanisms underlying PCD are conserved in animal and plant systems. 79,80 Experimental evidence of these conserved mechanisms include caspase-like activities detected in various plant cell-death model systems, the demonstration that expression of animal BAX can induce PCD in plants and yeast, and the identification of the plant BAX inhibitor-1 (BI-1) that can suppress cell death in both plants and animals. These strands of evidence indicate the existence of functional orthologs of BCL2, and its interacting proteins, in plants.…”

Section: Discussionmentioning

confidence: 99%

AtBAG6, a novel calmodulin-binding protein, induces programmed cell death in yeast and plants

et al. 2005

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Calmodulin (CaM) influences many cellular processes by interacting with various proteins. Here, we isolated AtBAG6, an Arabidopsis CaM-binding protein that contains a central BCL-2-associated athanogene (BAG) domain. In yeast and plants, overexpression of AtBAG6 induced cell death phenotypes consistent with programmed cell death (PCD). Recombinant AtBAG6 had higher affinity for CaM in the absence of free Ca 2 þ than in its presence. An IQ motif (IQXXXRGXXXR, where X denotes any amino-acid) was required for Ca 2 þ -independent CaM complex formation and single amino-acid changes within this motif abrogated both AtBAG6-activated CaM-binding and cell death in yeast and plants. A 134-amino-acid stretch, encompassing both the IQ motif and BAG domain, was sufficient to induce cell death. Agents generating oxygen radicals, which are known to be involved in plant PCD, specifically induced the AtBAG6 transcript. Collectively, these results suggest that AtBAG6 is a stress-upregulated CaM-binding protein involved in plant PCD.

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Section: Discussionmentioning

confidence: 99%

AtBAG6, a novel calmodulin-binding protein, induces programmed cell death in yeast and plants

et al. 2005

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“…9 Conversely, Bax-expression in plants caused localized tissue collapse in a manner resembling the hypersensitive response, a PCD response of plants in defense against pathogens. 10 To further understand the nature of the interactions of Bax with the yeast intracellular environment in eliciting cell death, we undertook the generation and characterization of a set of methane sulfonic acid ethyl ester (EMS)-mutagenized yeast strains that are tolerant to Bax expression. One of them was used in a genetic screen to isolate yeast genes restoring Bax sensitivity.…”

Section: Dear Editormentioning

confidence: 99%

Yeast mutants resistant to Bax lethality reveal distinct vacuolar and mitochondrial alterations

et al. 2004

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“…Other elements must be common, given recent evidence in which transgenic plants were constructed to express bcl-x L, an inhibitor of apoptosis, which also conferred protection against senescence and oxidative cell death in tobacco (Mitsuhara et al, 1999). In the converse experiment, plants expressing Bax, a pro-moter of animal cell death, appeared to activate an endogenous cell death response (Lacomme & Santa Cruz, 1999). Also, plant cells undergoing hypersensitive cell death can cleave poly(ADP-ribose) polymerase (PARP), an indicator of apoptotic cell death, through induction of cysteine protease activity (D'Silva et al, 1998).…”

Section: Summary Of Plant Cell Death Processesmentioning

confidence: 99%

Tansley Review No. 118

Kingston‐Smith

Theodorou

2000

New Phytologist

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It is generally assumed that breakdown of plant material in the rumen is a process mediated by gut microorganisms. This view arose because of the identification of a pre-gastric fermentation in the rumen, brought about by a large and diverse microbial population. The extensive use of dried and ground feed particles in forage evaluation might have helped to promote this assumption. However, although the assumption might be correct in animals feeding on conserved forage (hay and silage) where the cells of ingested forage are dead, it is possible that with grazed (living) forage, the role played by plant enzymes in the rumen has been overlooked. In a grazing situation, plant cells that remain intact on entering the rumen are not inert, but will respond to the perceived stresses of the rumen environment for as long as they are metabolically viable. Metabolic adjustments could include anaerobic and heat-shock responses that could promote premature senescence, leading to remobilization of cell components, especially proteins. Moreover, contact of plant cells with colonizing microorganisms in the rumen might promote a type of hypersensitive response, in much the same way as it does outside the rumen. After fresh plant material enters the rumen and prior to extensive plant cell-wall degradation, there is often a phase of rapid proteolysis providing N in excess of that required to maintain the rumen microbial population. The inefficient use of this ingested N results in generation of ammonia and urea in exhaled breath and urine, which promotes welfare and environmental pollution concerns. Therefore an important research goal in livestock agriculture is to find ways of decreasing this initial rate of proteolysis in the rumen. This will benefit the farmer financially (through decreased use of feed supplements), but will also benefit the environment, as N pollution can adversely affect pasture diversity and ecology. This review considers the possible responses of plant metabolism to the rumen environment, and how such considerations could alter current thinking in ruminant agriculture.

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Bax-induced cell death in tobacco is similar to the hypersensitive response

Cited by 399 publications

References 50 publications

AtBAG6, a novel calmodulin-binding protein, induces programmed cell death in yeast and plants

AtBAG6, a novel calmodulin-binding protein, induces programmed cell death in yeast and plants

Yeast mutants resistant to Bax lethality reveal distinct vacuolar and mitochondrial alterations

Tansley Review No. 118

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