A Multigene Family of Trypsin/α-Amylase Inhibitors from Cereals

Carbonero, Pilar; Garcı́a-Olmedo, Francisco

doi:10.1007/978-94-011-4431-5_26

Cited by 48 publications

(47 citation statements)

References 50 publications

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“…The impressive conformational stability of LDI together with possibility for integration with redox regulatory networks provides a possible rationale for conservation of the structural scaffold of the CTIs through a divergent evolution of the individual protein subfamilies. The outcome of this is a multitude of roles played by CTIs in regulation of plant development as seen in the present study and for previously described defense mechanisms (53).…”

Section: Ldi Loop 1 Involvement In Protein-proteinsupporting

confidence: 67%

Crystal Structure of Barley Limit Dextrinase-Limit Dextrinase Inhibitor (LD-LDI) Complex Reveals Insights into Mechanism and Diversity of Cereal Type Inhibitors

Møller

Vester-Christensen

Jensen

et al. 2015

Journal of Biological Chemistry

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Background: Barley limit dextrinase (LD), the sole starch debranching enzyme active during seed germination, is regulated by an endogenous inhibitor (LDI). Results: The crystal structure of the LD-LDI complex reveals a new and unexpected binding mode among cereal type inhibitors. Conclusion: A hydrophobic cluster drives the picomolar affinity of LDI. Significance: The molecular understanding of regulation of starch mobilization during germination is augmented.

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Section: Ldi Loop 1 Involvement In Protein-proteinsupporting

confidence: 67%

Crystal Structure of Barley Limit Dextrinase-Limit Dextrinase Inhibitor (LD-LDI) Complex Reveals Insights into Mechanism and Diversity of Cereal Type Inhibitors

Møller

Vester-Christensen

Jensen

et al. 2015

Journal of Biological Chemistry

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“…These proteins had been previously characterized [5,17,32], and their role as insecticides and acaricides supported by in vitro assays against digestive proteases from insects and acari, and by in vivo assays using transformed plants expressing some of the cystatins and the BTI-CMe protein [10,11,[33][34][35][36]. However, their inhibitory capacity towards plant bacterial and fungal pathogens had been less characterized.…”

Section: Discussionmentioning

confidence: 99%

“…Then, they were classified as cysteine, Abbreviations: PhyCys, plant cystatins; ORF, open reading frame; EC 50 , effective concentration for 50% inhibition; BTI, barley trypsin inhibitor; CPI, cystatin protease inhibitor. serine, aspartic, and metalloprotease inhibitors [2], However, several homologous inhibitors are able to inhibit different kind of proteases and they are now classified in function of their sequence similarities and tridimensional structures [3], Two of the most abundant plant protease inhibitors are the cystatins, family 125, that are cysteine protease inhibitors, and the cereal trypsin/ a-amylase inhibitors, family 16 [4,5], Plant cystatins (PhyCys) are plant proteinaceous inhibitors of cysteine proteases of the papain CIA family integrated in an independent subfamily on the cystatin phylogenetic tree [6,7], The cystatin inhibitory mechanism is produced by a tight and reversible interaction with their target enzymes. It involves a tripartite wedge formed by the partially flexible N-terminus containing a glycine residue and two hairpin loops carrying a conserved QxVxG motif and a tryptophan residue, respectively.…”

Section: Introductionmentioning

confidence: 99%

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Differential in vitro and in vivo effect of barley cysteine and serine protease inhibitors on phytopathogenic microorganisms

Carrillo¹,

Herrero²,

Cambra³

et al. 2011

Plant Physiology and Biochemistry

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Keywords:Cysteine protease inhibitor Serine protease inhibitor Barley Plant pathogen Transgenic plant Protease inhibitors from plants have been involved in defence mechanisms against pests and pathogens. Phytocystatins and trypsin/a-amylase inhibitors are two of the best characterized protease inhibitor families in plants. In barley, thirteen cystatins (HvCPI-1 to 13) and the BTI-CMe trypsin inhibitor have been previously studied. Their capacity to inhibit pest digestive proteases, and the negative in vivo effect caused by plants expressing these inhibitors on pests support the defence function of these proteins. Barley cystatins are also able to inhibit in vitro fungal growth. However, the antifungal effect of these inhibitors in vivo had not been previously tested. Moreover, their in vitro and in vivo effect on plant pathogenous bacteria is still unknown. In order to obtain new insights on this feature, in vitro assays were made against different bacterial and fungal pathogens of plants using the trypsin inhibitor BTI-CMe and the thirteen barley cystatins. Most barley cystatins and the BTI-CMe inhibitor were able to inhibit mycelial growth but no bacterial growth. Transgenic Arabidopsis plants independently expressing the BTI-CMe inhibitor and the cystatin HvCPI-6 were tested against the same bacterial and fungal pathogens. Neither the HvCPI-6 expressing transgenic plants nor the BTI-CMe ones were more resistant to plant pathogen fungi and bacteria than control Arabidopsis plants. The differences observed between the in vitro and in planta assays against phytopathogenic fungi are discussed.

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“…They are categorized according to their amino acid or nucleotide sequence. The main protease inhibitors present in barley seeds are the following: a bifunctional barley α-amylase/subtilisin inhibitor (BASI), chymotrypsin/subtilisin inhibitors 1 and 2 (CI-1 and CI-2), a barley Bowman-Birk type trypsin inhibitor (BBBI), a large group of inhibitors representing bifunctional α-amylase/trypsin inhibitors (CM proteins) and serpins 43,305 . Each family contains members differing in enzyme specificities 43,305 .…”

Section: Protease Inhibitors (Pis) (Pr-6)mentioning

confidence: 99%

A Review: Biological and Technological Functions of Barley Seed Pathogenesis-Related Proteins (PRs)

Gorjanović

2009

Journal of the Institute of Brewing

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The mature barley seed proteome is dominated by proteins involved in stress responses, including the Pathogenesis-Related proteins (PRs). PRs are currently classified into 17 families. The biochemistry of the PRs families, whose members are constitutively present in barley seed, is surveyed in this paper. These proteins are assumed to protect dormant and germinating seeds against pathogenic microorganisms and pests. The current knowledge on PRs structural and functional properties is summarized in an attempt to illustrate their importance in barley seed innate resistance. At the same time, a platform to understand PRs technological function in cereal foods and in beverage processing and quality is provided.

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A Multigene Family of Trypsin/α-Amylase Inhibitors from Cereals

Cited by 48 publications

References 50 publications

Crystal Structure of Barley Limit Dextrinase-Limit Dextrinase Inhibitor (LD-LDI) Complex Reveals Insights into Mechanism and Diversity of Cereal Type Inhibitors

Crystal Structure of Barley Limit Dextrinase-Limit Dextrinase Inhibitor (LD-LDI) Complex Reveals Insights into Mechanism and Diversity of Cereal Type Inhibitors

Differential in vitro and in vivo effect of barley cysteine and serine protease inhibitors on phytopathogenic microorganisms

A Review: Biological and Technological Functions of Barley Seed Pathogenesis-Related Proteins (PRs)

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