The Pathogenesis-Related Proteins of Plants

Carr, John P.; Klessig, Daniel F.

doi:10.1007/978-1-4615-7084-4_5

Cited by 66 publications

(49 citation statements)

References 208 publications

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“…These proteins were identified as GLPs, CLPs, and TLPs (Hon et al, 1995). Similar proteins, endo-P-1,3-glucanases, endochitinases, and TLPs, are known to be related to the mechanism for plant disease resistance (Carr and Klessig, 1989;Bol et al, 1990;Collinge et al, 1993;Stintzi et al, 1993) and are therefore classified as PR proteins. Proteins similar to PR proteins are also induced by other conditions unrelated to pathogen induction, such as ethylene (Boller et al, 1983), UV light (Yalpani et al, 1994), ozone (Ernst et al, 1992;Karenlampi et al, 1994;Yalpani et al, 1994), high salt (Esaka et al, 1994), heat (Margis-Pinheiro et al, 1994), phytotoxic metals (Jacobsen et al, 1992), and wounding (Zhang and Punja, 1994).…”

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confidence: 99%

Immunolocalization of Antifreeze Proteins in Winter Rye Leaves, Crowns, and Roots by Tissue Printing

et al. 1996

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During cold acclimation, antifreeze proteins (AFPs) that are similar to pathogenesis-related proteins accumulate in the apoplast of winter rye (Secale cereale L. cv Musketeer) leaves. AFPs have the ability to modify the growth of ice. To elucidate the role of AFPs in the freezing process, they were assayed and immunolocalized in winter rye leaves, crowns, and roots. Each of the total soluble protein extracts from cold-acclimated rye leaves, crowns, and roots exhibited antifreeze activity, whereas no antifreeze activity was observed in extracts from nonacclimated rye plants. Antibodies raised against three apoplastic rye AFPs, corresponding to a glucanase-like protein (CLP, 32 kD), a chitinase-like protein (CLP, 35 kD), and a thaumatin-like protein (TLP, 25 kD), were used in tissue printing to show that the AFPs are localized in the epidermis and in cells surrounding intercellular spaces in cold-acclimated plants. Although GLPs, CLPs, and TLPs were present in nonacclimated plants, they were found in different locations and did not exhibit antifreeze activity, which suggests that different isoforms of pathogenesis-related proteins are' produced at low temperature. The location of rye AFPs may prevent secondary nucleation of cells by epiphytic ice or by ice propagating through the xylem. l h e distributions of pathogenesis-induced and cold-accumulated CLPs, CLPs, and TLPs are similar and may reflect the common pathways by which both pathogens and ice enter and propagate through plant tissues.

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confidence: 99%

Immunolocalization of Antifreeze Proteins in Winter Rye Leaves, Crowns, and Roots by Tissue Printing

et al. 1996

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“…14), peroxidases (13) f-I,3 glucanases and chitinases (1), hydroxyproline-rich glycoproteins (25), and a diverse group of acidic, extracellular proteins known collectively as PR' proteins (reviewed in ref. 4). Among the proteins having known enzymatic function, the A-1 ,3-glucanases are particularly interesting because they are hormonally and developmentally regulated in uninfected plants (7,18) and are thought to protect plants from fungal infection ( A role of fl-1,3-glucanases in plant defense is suggested by the observation that #-1,3-glucanases and endochitinases are coordinately induced as part of the hypersensitive response to pathogen infection (17,28).…”

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confidence: 99%

“…These proteins are not found in healthy tissues but accumulate to high levels in response to pathogen infection and treatment with certain chemical inducers such as aspirin (reviewed in ref. 4). To date, one class III enzyme has been identified, PR-Q' (9,21), an acidic protein that also accumulates in the apoplast when infected with a pathogen.…”

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confidence: 99%

Differential Regulation of β-1,3-Glucanase Messenger RNAs in Response to Pathogen Infection

Ward¹,

Payne²,

Moyer³

et al. 1991

Plant Physiol.

147

102

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The acidic, extracellular, glucan endo-1,3-t8-glucosidases (EC 3.2.1.39; j0-1,3-glucanases), pathogenesis-related proteins-2, -N, and -O (i.e. PR-2, PR-N, and PR-0) were purified from Nicotiana tabacum (tobacco) and their partial amino acid sequences determined. Based on these data, complementary DNA (cDNA) clones encoding the proteins were isolated. Additional cDNAs were isolated that encoded proteins approximately 90% identical with PR-2, PR-N, and PR-0. Although the proteins encoded by these cDNAs have not been identified, their deduced amino acid sequences have slightly basic or neutral calculated isoelectric points, as well as carboxy-terminal extensions. These physical characteristics are shared by the vacuolar form of ,B-1,3-glucanase and other vacuolar localized analogs of PR proteins, suggesting that the unidentified proteins may be similarly localized.A preliminary evolutionary model that separates the fl-1,3-glucanase gene family from tobacco into at least five distinct subfamilies is proposed. The expression of ,-1,3-glucanase messenger RNAs (mRNAs) in response to infection by tobacco mosaic virus was examined. Messages for the acidic glucanases were induced similarly to the mRNAs for other PR proteins. However, the basic glucanase showed a different response, suggesting that different isoforms are differentially regulated by tobacco mosaic virus infection at the mRNA level.

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“…To (3). Therefore, the suppression of some woundinducible genes by SA is probably to minimize unnecessary induction of these proteins that are not beneficial for the defense response to pathogen.…”

Section: Analysis Of Deletion Mutantsmentioning

confidence: 99%

“…Among several molecules that have been proposed as endogenous signals for the defense response to pathogens (3,4,25,30), SA2 was recognized as a key molecule that triggers local and systemic responses of tobacco to viral infection (14,15,19,27,29). SA levels in resistant, but not in susceptible, tobacco increase drastically in both TMVinfected and uninfected leaves in the same plant (15).…”

mentioning

confidence: 99%

Inhibition of Sucrose Enhancer Effect of the Potato Proteinase Inhibitor II Promoter by Salicylic Acid

Kim¹,

Kim²,

Costa³

et al. 1992

Plant Physiol.

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Effect of salicylic acid (SA) on the expression of the potato proteinase inhibitor (PI) II promoter was studied with transgenic tobacco plants (Nicotlana tabacum) carrying a gene fusion between the Pl-l1 promoter and the chloramphenicol acetyltransferase (cat) reporter. As previously observed, the P-1l promoter was inducible by wounding and the promoter activity was further enhanced by sucrose. Addition of SA did not influence the wound induction of the Pl-l1 promoter but significantly inhibited the sucrose response. The 5'-deletion mutant -573 was unable to respond to wounding but did respond to sucrose and SA. The 3'-deletion analysis indicated the presence of a sucrose-responsive element between -574 and -520. A study of the insertion mutants revealed the function of another sucrose-responsive element between -522 and -500. Enhancer effects of these sucroseresponsive elements were inhibited by SA. These studies suggest that SA inhibits Pl-l1 promoter activity by decreasing the sucrose response. Analysis of SA-related chemicals revealed that only acetyl-SA showed a similar inhibitory effect, and other hydroxybenzoic acids had little or no effect on the sucrose enhancer activity. Therefore, it seems that the interaction between SA and the receptor molecule is specific.

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The Pathogenesis-Related Proteins of Plants

Cited by 66 publications

References 208 publications

Immunolocalization of Antifreeze Proteins in Winter Rye Leaves, Crowns, and Roots by Tissue Printing

Immunolocalization of Antifreeze Proteins in Winter Rye Leaves, Crowns, and Roots by Tissue Printing

Differential Regulation of β-1,3-Glucanase Messenger RNAs in Response to Pathogen Infection

Inhibition of Sucrose Enhancer Effect of the Potato Proteinase Inhibitor II Promoter by Salicylic Acid

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