Gene structure and in situ transcript localization of pathogenesis-related protein 1 in parsley

Somssich, Imre E.; Schmelzer, Elmon; Kawalleck, Petra; Hahlbrock, Klaus

doi:10.1007/bf00333403

Cited by 201 publications

(164 citation statements)

References 31 publications

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“…In addition, two chitinases and two j3-glucanases showing differential regulation during development and in response to fungal infection have been described in pea tissue (16). Transcripts of some defence genes (HRGP, PR 1) have been shown to accumulate in areas distant to the site of infection whereas others may be more localized (23,24). It is our intention to investigate spatial and temporal aspects of the regulation of expression of the genes for the hydrolytic enzymes in Brassica which we believe to underlie the changes in activity reported here.…”

Section: Discussionmentioning

confidence: 99%

Induction of Hydrolytic Enzymes in Brassica campestris in Response to Pathovars of Xanthomonas campestris

Conrads-Strauch

Dow²,

Milligan³

et al. 1990

Plant Physiol.

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Inoculation of mature leaves of turnip (Brassica campestris) with the incompatible Xanthomonas campestris pv vitians resulted in the induction of 83-1,3-glucanase and chitinase/lysozyme (CHL) activity. No increase in the basal activity of 8-1,3-glucanase was observed after inoculation of leaves with heat-or nfampicin-killed X. c. vitians, Escherichia coii, or sterile water. Inoculation with the compatible X. campestris pv campestris resulted in a slower induction of glucanase than that seen with X. c. vitians. In contrast, all bacteria caused an induction of CHL activity. One major ,-1,3-glucanase (molecular mass 36.5 kilodaltons, isoelectric point [pi] -8.5) was purified from both inoculated and untreated leaves by ion-exchange chromatography. The enzyme degraded laminarin by an endo-glycolytic mechanism. Two major CHL isozymes (CHL 1 and CHL 2, molecular mass 30 kilodaltons and pi 9.4 and 10.2, respectively) were purified from X. c. vitians inoculated leaves by affinity chromatography on a chitin column followed by ion-exchange chromatography. Both enzymes degraded chitin by an endo-glycolytic mechanism although the ratio of lysozyme to chitinase specific activities for CHL 1 and CHL2 were different. The induction of CHL 1 was associated with the hypersensitive reaction caused by X. c. vitians whereas all other treatments induced largely CHL 2.gens. All plant lysozymes so far described have been shown to act as endochitinases (3). (3-1,3-Glucanase and chitinase are coordinately induced in a number of plant tissues by pathogen attack and elicitors (25).We are interested in the mechanisms of resistance of Brassica spp., in particular turnip (Brassica campestris) to incompatible pathovars of the Gram-negative phytopathogen Xanthomonas campestris. X. campestris pv campestris (hereafter referred to as X. c. campestris) is an important worldwide pathogen of almost all cultivated brassicas and noncrop crucifers (27) whereas X. c. vitians, a pathogen of lettuce (Lactuca sativa) is incompatible with brassica and triggers HR characterized by tissue collapse (6). As part of our study on defence mechanisms in Brassica, we have investigated the induction of CHL and (3-1,3-glucanase in response to X. c. campestris, X. c. vitians, and Escherichia coli (a nonpathogen). Lysozyme activity in turnip was originally described by Fleming (10) and the enzymes from turnip root (1) and cauliflower (9) have been partially characterized. In this paper we report on the characterization of the (-1,3-glucanase and of isoforms of CHL that show differential regulation in response to the different bacteria.The induction of the hydrolytic enzymes (3-1,3-glucanase and chitinase has been studied in a number of plants in response to infection, heat-killed pathogens, pathogen cell walls, or wounding (2,3,11). Some of the PR2 proteins induced in several different plants in response to infection have now been identified as (3-1,3-glucanases and chitinases (12,13,18). These hydrolases are of interest as plant defence products because of their...

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Section: Discussionmentioning

confidence: 99%

Induction of Hydrolytic Enzymes in Brassica campestris in Response to Pathovars of Xanthomonas campestris

Conrads-Strauch

Dow²,

Milligan³

et al. 1990

Plant Physiol.

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show abstract

“…Several lines of evidence suggest that this group of PR proteins are intraceliular (Somssich et al, 1988;Warner et al, 1992) and thus differ from the 'classical' acidic PR proteins described from tobacco which are generally extracellular . The AoPR1 promoter was fused to the I~-glucuronidase (GUS) reporter gene and used to transform tobacco.…”

Section: Introductionmentioning

confidence: 87%

“…PcPRI-1 is a parsley gene coding for a member of the intracellular PR group of proteins which has been shown to be strongly upregulated at sites of fungal attack and following microbial elicitor treatment of established suspension cultured cells (Meier et al, 1991 ;Somssich et al, 1988). Although there are no significant long stretches of homology between the AoPR1 and PcPRI-1 promoters there is a sequence from -396 to -388 in the AoPR1 promoter that is identical to an inducible footprinted sequence of the PcPRI-1 promoter from -244 to -235 which reads ATTTGACCG ( Figure 5).…”

Section: The Aopr1 Promoter Contains Elements Related To Nucleotide Smentioning

confidence: 99%

The developmental expression of the asparagus intracellular PR protein (AoPR1) gene correlates with sites of phenylpropanoid biosynthesis

Warner

Gill

Draper³

1994

The Plant Journal

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“…A local HR is often associated with the onset of systemic acquired resistance (SAR; Chester, 1933;Enyedi et al, 1992;Ryals et al, 1994Ryals et al, , 1996, in this issue) in dista1 plant tissues. In addition, sites of the HR are invariably focal points for transcriptional induction of plant defense genes in neighboring cells (Somssich et al, 1988;Schmelzer et al, 1989). Subsequent biosynthesis of protective secondary metabolites and cell wall buttressing around the HR site are also thought to contribute to overall pathogen containment.…”

Section: Introductionmentioning

confidence: 99%

Death Don't Have No Mercy: Cell Death Programs in Plant-Microbe Interactions.

1996

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Gene structure and in situ transcript localization of pathogenesis-related protein 1 in parsley

Cited by 201 publications

References 31 publications

Induction of Hydrolytic Enzymes in Brassica campestris in Response to Pathovars of Xanthomonas campestris

Induction of Hydrolytic Enzymes in Brassica campestris in Response to Pathovars of Xanthomonas campestris

The developmental expression of the asparagus intracellular PR protein (AoPR1) gene correlates with sites of phenylpropanoid biosynthesis

Death Don't Have No Mercy: Cell Death Programs in Plant-Microbe Interactions.

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