Pathogenesis-related proteins of tomato: II. Biochemical and immunological characterization

Fischer, W.; Christ, Urs; Baumgartner, Monika; Erismann, Karl Hans; Mösinger, Egon

doi:10.1016/0885-5765(89)90008-8

Cited by 36 publications

(20 citation statements)

References 24 publications

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“…Our finding that JIPs 23 and 10/12 are composed of several proteins is in agreement with an earlier report (Mueller-Uri et al, 1988). Immunoblots of IWF-localized JIPs and PR proteins were probed with an antiserum raised against a PR protein of group 1 (P14 of tomato, Fischer W et al, 1989). The antiserum detected a barley protein of 16 kD (Fig.…”

Section: Results Local Protedion Of Barley By Jasupporting

confidence: 80%

Effect of Jasmonic Acid on the Interaction of Barley (Hordeum vulgare L.) with the Powdery Mildew Erysiphe graminis f.sp. hordei

Schweizer¹,

Gees²,

Mösinger³

1993

Plant Physiol.

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Section: Results Local Protedion Of Barley By Jasupporting

confidence: 80%

Effect of Jasmonic Acid on the Interaction of Barley (Hordeum vulgare L.) with the Powdery Mildew Erysiphe graminis f.sp. hordei

Schweizer¹,

Gees²,

Mösinger³

1993

Plant Physiol.

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“…Its NH 2 -terminal amino acid sequence beginning with a pair of threonine residues is highly similar to the amino termini that were determined for the mature, active cucumisin (7), P69 (15,31), lim9 (12), and macluralisin (11). Apparently, the processing site at the junction between the prodomain and the catalytic domain is well conserved in plant subtilases (18).…”

Section: Discussionmentioning

confidence: 96%

“…Subtilases typically comprise a prodomain, which assists in the folding of the protease and serves as an intramolecular inhibitor of enzymatic activity (1,30). For cucumisin (7), P69 (31), and the lily subtilase lim9 (12), the NH 2 termini of the mature enzymes have been determined and were found to be well conserved, beginning with an invariable pair of threonine residues. This sequence motif is also found in LeSBT1 (Fig.…”

Section: Molecularmentioning

confidence: 99%

LeSBT1, a Subtilase from Tomato Plants

Janzik

Macheroux

Amrhein

et al. 2000

Journal of Biological Chemistry

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The cDNA of a tomato subtilase designated LeSBT1 was cloned from a tomato flower cDNA library. The deduced amino acid sequence indicated for LeSBT1 the structure of a prepro-protein targeted to the secretory pathway by virtue of an amino-terminal signal peptide. LeSBT1 was expressed in the baculovirus/insect cell system and a processed 73-kDa form of LeSBT1, lacking both signal peptide and prodomain, was purified to homogeneity from culture supernatants. This 73-kDa LeSBT1, however, lacked proteolytic activity. Zymogen activation to yield 68-kDa LeSBT1 required the additional processing of an amino-terminal autoinhibitory peptide in a strictly pH-dependent manner. Mature 68-kDa LeSBT1 showed highest activity at acidic pH consistent with its presumed localization in the apoplast of the plant cell. In comparison to other plant subtilases, LeSBT1 exhibited a narrower substrate specificity in that it cleaves only polypeptide substrates preferentially but not exclusively carboxyl-terminal of glutamine residues. The possible involvement of LeSBT1 in selective proprotein processing is discussed with reference to the related mammalian proprotein convertases.

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“…Recently, a possible biological function has been ascribed to some of the tomato PR proteins (11,17,28). Although there is no evidence for a possible role of P2, P4, and P6 in disease resistance, the early induction of these proteins in incompatible tomato-C. fulvum interactions justifies further research.…”

Section: Purification Of the Basic 15-kd Pr Proteinsmentioning

confidence: 99%

Purification and Serological Characterization of Three Basic 15-Kilodalton Pathogenesis-Related Proteins from Tomato

Joosten

Bergmans²,

Meulenhoff³

et al. 1990

Plant Physiol.

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In tomato (Lycopersicon esculentum) several acidic and basic apoplastic pathogenesis-related (PR) proteins are induced upon inoculation with virulent or avirulent races of Cladosporium fulvum (Cooke) (syn. Fulvia fulva [Cooke] Cif). One of the most predominant and best characterized tomato PR proteins is P14, a basic protein that shows homology to the tobacco (Nicotiana tabacum) PR-1 protein family. To investigate whether, by analogy with these tobacco PR-1 proteins, P14 also belongs to a family of differently charged isomers, the abundantly occurring PR proteins with molecular masses around 15 kilodaltons (kD) were purified from apoplastic fluids isolated from C. fulvum-infected tomato. Three basic proteins migrating similarly to P14 on sodium dodecyl sulfate polyacrylamide gels were purified to homogeneity by gel filtration followed by high resolution liquid chromatography. Two proteins (15.5 kD, isoelectric point [pi] 10.9 and 10.7 appeared to be serologically related to each other and to the tobacco PR-1 proteins. A third protein (15 kD, pi 10.4) was not serologically related to any other tomato PR protein but was found to be related to PR-R from tobacco.

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Pathogenesis-related proteins of tomato: II. Biochemical and immunological characterization

Cited by 36 publications

References 24 publications

Effect of Jasmonic Acid on the Interaction of Barley (Hordeum vulgare L.) with the Powdery Mildew Erysiphe graminis f.sp. hordei

Effect of Jasmonic Acid on the Interaction of Barley (Hordeum vulgare L.) with the Powdery Mildew Erysiphe graminis f.sp. hordei

LeSBT1, a Subtilase from Tomato Plants

Purification and Serological Characterization of Three Basic 15-Kilodalton Pathogenesis-Related Proteins from Tomato

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