Circadian expression and induction by wounding of tobacco genes for cysteine proteinase

Linthorst, Huub J. M.; Does, Chris van der; Brederode, Frans Th.; Bol, John F.

doi:10.1007/bf00014551

Cited by 81 publications

(71 citation statements)

References 24 publications

(29 reference statements)

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“…More recently, other types of proteinases (or their cDNAs) have been shown to be induced by insect feeding, mechanical wounding, or pathogen attack. These include leucine aminopeptidase (Pautot et al, 1993;Chao et al, 1999), a subtilisin-like proteinase (Jorda et al, 1999), carboxypeptidase (Metha et al, 1996), and aspartic peptidase (Schaller and Ryan, 1996) in tomato and cysteine proteinase in tobacco (Linthorst et al, 1993).…”

Section: Discussionmentioning

confidence: 99%

A Unique 33-kD Cysteine Proteinase Accumulates in Response to Larval Feeding in Maize Genotypes Resistant to Fall Armyworm and Other Lepidoptera

et al. 2000

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Plants respond to insect feeding with a number of defense mechanisms. Using maize genotypes derived from Antiquan germ plasm that are resistant to Lepidoptera, we have demonstrated that a unique 33-kD cysteine proteinase accumulates in the whorl in response to larval feeding. The abundance of the proteinase increased dramatically at the site of larval feeding after 1 hr of infestation and continued to accumulate for as long as 7 days. The 33-kD cysteine proteinase was most abundant in the yellow-green portion of the whorl-the normal site of larval feeding and the tissue that has the greatest inhibitory effect on larval growth in bioassays. The proteinase was expressed in response to wounding and was found in senescent leaves. It may be a marker of programmed cell death. The gene coding for the proteinase, mir1 , has been transformed into Black Mexican Sweet callus. When larvae were reared on callus expressing the proteinase, their growth was inhibited ‫ف‬ 60 to 80%. The expression of a cysteine proteinase, instead of a cysteine proteinase inhibitor, may be a novel insect defense mechanism in plants. INTRODUCTIONOver the past 25 years, maize inbreds resistant to feeding by larvae of numerous lepidopteran species have been developed from Antiguan germ plasm (Williams and Davis, 1982;Williams et al., 1990a). Inbreds derived from this germ plasm (Mp704 and Mp708) are resistant to feeding by fall armyworm ( Spodoptera frugiperda ), southwestern corn borer ( Diatraea grandiosella), European corn borer ( Ostinia nubilalis ), sugarcane borer ( D. saccharalis), tobacco budworm ( Heliothis virescens ), corn earworm ( Helicoverpa zea ), and other Lepidoptera. Fall armyworm larvae feed extensively on whorl leaf tissue, often resulting in crop losses. Genetic and quantitative trait loci analyses indicate that resistance to these Lepidoptera is a quantitative trait regulated by several genes (Williams et al., 1989;Khairallah et al., 1998). Traits such as high hemicellulose content, low protein content, and leaf toughness appear to be correlated with reduced larval growth (Williams et al., 1998). No studies have indicated conclusively that secondary products contribute to the resistance, but two-dimensional gel electrophoresis has indicated that the presence of 36-and 21-kD proteins in the whorl may be predictive of resistance (Callahan et al., 1992).Bioassays in which fall armyworm larvae are reared on lyophilized whorl tissues indicate that larvae reared on resistant material weigh ‫ف‬ 50% less than those reared on susceptible material (Williams et al., 1990b). Larvae reared on lyophilized whorl tissue from resistant genotypes are smaller, grow more slowly, and pupate later than those reared on similar material from susceptible genotypes (Chang et al., 2000). The major effect of this germplasm is to slow larval growth and development and to increase the amount of time larvae are vulnerable to predators and parasites.The same phenotype, a 50% reduction in larval growth, is apparent when larvae are reared on nonfriable callus ...

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Section: Discussionmentioning

confidence: 99%

A Unique 33-kD Cysteine Proteinase Accumulates in Response to Larval Feeding in Maize Genotypes Resistant to Fall Armyworm and Other Lepidoptera

et al. 2000

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“…In some cases, these genes encode proteins with known functions, such as high mobility group DNA binding protein 1 from P. nil (Zheng et al, 1993), cysteine protease 8 from tobacco (Linthorst et al, 1993), CCRl and CCR2 from Arabidopsis (Carpenter et al, 1994), germinlike protein from mustard (Heintzen et al, 1994a), glycine-rich RNA binding proteins l a and 2a from mustard (Heintzen et al, 1994b), ADP-ribosylation factor 1 from C.…”

Section: Other Clock-controlled Genesmentioning

confidence: 99%

Coordination of Plant Metabolism and Development by the Circadian Clock.

Kreps

Kay

1997

Plant Cell

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“…Specific proteases are upregulated during senescence (Feller, 1986). There are everincreasing examples of the involvement of cysteine proteases during senescence and other cell death pathways (Linthorst et al, 1993 ;Smart, 1994 ;Valpuesta et al, 1995 ;Griffiths et al, 1997 ;Guerrero et al, 1998 ;Popovic et al, 1998 ;Sokolenko et al, 1998 ;Thomas & Donnison, 2000). It is interesting to note that cysteine proteases from plants are often inactivated on extraction, due to the presence of air (Yonezawa et al, 1997) ; this is not a problem if cysteine proteases are liberated into the anaerobic rumen fluid.…”

Section: Senescence In the Rumen ?mentioning

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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Circadian expression and induction by wounding of tobacco genes for cysteine proteinase

Cited by 81 publications

References 24 publications

A Unique 33-kD Cysteine Proteinase Accumulates in Response to Larval Feeding in Maize Genotypes Resistant to Fall Armyworm and Other Lepidoptera

A Unique 33-kD Cysteine Proteinase Accumulates in Response to Larval Feeding in Maize Genotypes Resistant to Fall Armyworm and Other Lepidoptera

Coordination of Plant Metabolism and Development by the Circadian Clock.

Tansley Review No. 118

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