The complete amino acid sequence of the pathogenesis-related (PR2) protein induced in chemically stressed bean leaves

Awade, Abalo; Metz-Boutigue, Marie Hélène; Ret, Monique Le; Génot, Geneviève; Amiri, Iradj; Burkard, G.

doi:10.1016/0167-4838(91)90064-7

Cited by 18 publications

(8 citation statements)

References 25 publications

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“…Copper treatment increased the level in roots, and the 50 mM Cu treatment made it visible also in the primary leaves. Awade et al (1991) reported the complete sequence of a mercuric chloride inducible PR2 protein in bean leaves; the sequence is identical to that of PvPR1.…”

Section: Discussionmentioning

confidence: 89%

Analysis of bean (Phaseolus vulgaris L.) proteins affected by copper stress

Cuypers

Koistinen

Kokko

et al. 2005

Journal of Plant Physiology

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Section: Discussionmentioning

confidence: 89%

Analysis of bean (Phaseolus vulgaris L.) proteins affected by copper stress

Cuypers

Koistinen

Kokko

et al. 2005

Journal of Plant Physiology

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“…Accumulating evidences indicate that pathogenesis-related proteins (PRs) might be synthesised in plant cells in response to diverse abiotic factors: paraquat, sodium phosphate and salicylic acid (Walter et al 1990;Awade et al 1991), abscisic acid (BarrattClark 1991Iturriaga et al 1994), ozone (Pääkkönen et al 1998), drought stress (Pääkkönen et al 1998;Hashimoto et al 2004), salinity (Hashimoto et al 2004;Srivastava et al 2004), wounding and cold-hardening (Liu et al 2005). Recent work has demonstrated that tolerance of tobacco plants to cadmium and mercury was obtained by the overexpression of a pepper basic PR 1 protein gene (Sarowar et al 2005).…”

Section: Discussionmentioning

confidence: 99%

Organospecific responses of lupin seedlings to lead Localization of hydrogen peroxide and peroxidase activity

2007

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In an earlier work using tissue printing method, we found that the PR-10 stress protein was observed in leaf petiole of lupin seedling where lead was not detected (Przymusiński et al. 2001). These results suggested the presence of substance(s) mediating a signal transduction from directly affected cells to distant organs. As the hydrogen peroxide was found to be involved in signal transduction pathway, in the present paper, we analysed the level of H 2 O 2 in the organ of lupin seedlings exposed to Pb 2+ with spectrophotometric method and tissue printing technique. It was unequivocally demonstrated that the level of H 2 O 2 and the activity of peroxidase increased in every tested organ of lead-treated lupin seedling. Both the level of H 2 O 2 and the activity of POX were correlated with amount of Pb 2+ ions in the cells (Przymusiński et al. 2001) and decreased in tissues more and more distant from the site of metal application. On the other hand, there was no correlation between the histological localization of H 2 O 2 and peroxidase. Our results seem to confirm the hypothesis that H 2 O 2 may act as a signalling substance involved in the induction of PR protein synthesis. It was indicated that there is high degree of correlation between the localization of H 2 O 2 and the histological localization of PR-10 proteins (Przymusiński et al. 2001) in every tested organ of lupin seedling. The presented hypothesis is also supported by the fact that H 2 O 2 and PR-10 proteins are detected in organs and tissues where Pb 2+ was not found at all.

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“…1 demonstrates that they are 56~o identical. A search within the nucleotide and protein sequence databases revealed that ABR17 and ABR18 were similar to the pea disease resistance response proteins Psdrrl, Psdrra and Psdrrg [13,7], and to pathogenesis-related proteins from bean (PvPRpl and PvPRp2, [27,1 ]), potato (pSTH-2 and pSTH-21, [18,19]) and parsley (PcPRI-1, PcPR1-2 and PcPR1-3, [26,15]. Wound-or stress-induced proteins from soybean (H4 and Sam22, [9]) and asparagus (AoPR1 [29]), as well as the major birch pollen allergen [ 6], also showed similarity with the ABR17 and ABR18 sequences.…”

Section: Gatcaaggaag Cacaaggagtcgaaattatcgaaggaaatggaggtccaggaaccatcamentioning

confidence: 99%

“…Another feature of the IPR proteins is that they are almost invariably part of gene families. The mRNAs corresponding to this class of proteins accumulate in response to pathogens or fungal elicitors in pea [13,7], bean [27,1], and parsley [26,15]. They have also been shown to accumulate in response to wounding and other stress in potato [18,19], soybean [9], and asparagus [29].…”

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confidence: 99%

Two ABA-responsive proteins from pea (Pisum sativum L.) are closely related to intracellular pathogenesis-related proteins

et al. 1994

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We report here the isolation of cDNAs encoding two abscisic acid-responsive pea (Pisum sativum L.) proteins, ABR17 and ABR18, which are synthesized during late seed development in vivo. Southern blot analyses suggest that ABR17 cDNA corresponds to a single-copy gene, but ABR18 is one member of a family of closely related sequences in the pea genome. The deduced amino acid sequences of ABR17 and ABR18 cDNAs showed similarity to those of the pea disease resistance response proteins, to pathogenesis-related and to stress-induced proteins in other species and to the major birch pollen allergen Betv1.

show abstract

The complete amino acid sequence of the pathogenesis-related (PR2) protein induced in chemically stressed bean leaves

Cited by 18 publications

References 25 publications

Analysis of bean (Phaseolus vulgaris L.) proteins affected by copper stress

Analysis of bean (Phaseolus vulgaris L.) proteins affected by copper stress

Organospecific responses of lupin seedlings to lead Localization of hydrogen peroxide and peroxidase activity

Two ABA-responsive proteins from pea (Pisum sativum L.) are closely related to intracellular pathogenesis-related proteins

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