Properties of Barley Seed Chitinases and Release of Embryo-Associated Isoforms during Early Stages of Imbibition

Swegle, Mark; Kramer, Karl J.; Muthukrishnan, Subbaratnam

doi:10.1104/pp.99.3.1009

Cited by 74 publications

(45 citation statements)

References 33 publications

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“…The arrowheads indicate ASP31. B, The same acid-soluble proteins as in A were transferred to nitrocellulose and detected using antisera against the major basic PR1 protein of tomato (Fischer et al, 1989; 1000-fold dilution) and against a barley PR3 protein (Swegle et al, 1992; 500-fold dilution), respectively. For INA concentrations, see "Materials and Methods.…”

Section: General Gene-expression Patternsmentioning

confidence: 99%

Gene-Expression Patterns and Levels of Jasmonic Acid in Rice Treated with the Resistance Inducer 2,6-Dichloroisonicotinic Acid

1997

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Section: General Gene-expression Patternsmentioning

confidence: 99%

Gene-Expression Patterns and Levels of Jasmonic Acid in Rice Treated with the Resistance Inducer 2,6-Dichloroisonicotinic Acid

1997

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“…There are several embryonic defense mechanisms, including the production of plant lectins and pathogen-related proteins in response to attacks by pathogens or insects (Swegle et al, 1992;Ye et al, 2001;Guiderdoni et al, 2002). A well-known defense component is Ser protease inhibitors.…”

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confidence: 99%

Molecular Cloning and Functional Analysis of a Novel Type of Bowman-Birk Inhibitor Gene Family in Rice

et al. 2003

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inhibitor (BBI) genes encode serine protease inhibitors that have repetitive cysteine-rich domains with reactive sites for the trypsin or chymotrypsin family. We have identified seven BBI genes from japonica rice (Oryza sativa subsp. japonica var Teqing). All of the genes identified were found in a single cluster on the southern end of the long arm of rice chromosome 1. Four of the seven BBI genes have two repetitive cysteine-rich domains, whereas one has a truncated domain with only one reactive site. We have also identified three novel BBI genes, each of which possesses three repetitive domains instead of two. In situ hybridization analyses indicated that the accumulation of rice BBI transcripts was differentially regulated in germinating embryos and also in the leaves, roots, and flower organs at later developmental stages. Different members of the rice BBI gene family displayed different expression patterns during rice seed germination, and wounding induced the expression of rice BBI transcripts. The three-domain BBIs had higher expression levels than the two-domain BBIs. It was also found that the mRNA of rice BBI genes was present in abundant amounts in scutellar epithelium and aleurone layer cells. RBBI3-1, one of the three-domain RBBI, exhibited in vitro trypsin-inhibiting activity but no chymotrypsin-inhibiting activity. Overexpression of RBBI2-3 in transgenic rice plants resulted in resistance to the fungal pathogen Pyricularia oryzae, indicating that proteinase inhibitors confer resistance against the fungal pathogen in vivo and that they might play a role in the defense system of the rice plant.Plants have developed defense systems to combat various pathogens throughout their life cycle, from the seed stage until senescence, and it is particularly important that the embryo be kept free from infection. There are several embryonic defense mechanisms, including the production of plant lectins and pathogen-related proteins in response to attacks by pathogens or insects (Swegle et al., 1992;Ye et al., 2001;Guiderdoni et al., 2002). A well-known defense component is Ser protease inhibitors. They are expressed in developing seeds and are thought to play an important role in inhibiting trypsin and chymotrypsin of external origin (Ryan, 1981). Two major Ser protease inhibitors have been studied extensively in plants: Kunitz inhibitors and Bowman-Birk inhibitors (BBIs; Ryan, 1990). BBIs are Cys-rich proteins of about 8 to 16 kD with disulfide bonds and are encoded by a family of related genes. The BBI gene family has been found in both the Fabaceae and the Poaceae. BBIs identified in Fabaceae, such as soybean (Glycine max) and lima bean (Phaseolus lunatus), are 8-kD proteins. They have one BBI domain with two reactive sites for trypsin and the related enzymes, such as chymotrypsin (Birk, 1987). These protease inhibitors are double-headed, with two reactive sites in a single inhibitor molecule. Interestingly, this type of inhibitor displays anticarcinogenic activity (Birk, 1993;Kennedy, 1993).The BBIs found in...

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“…A basic 26 kDa barley seed chitinase (CHI26) inhibited the growth of T. reesei and F. sporotrichioides both by itself and also synergistically with glucanase and RIP 181 . Embryo-associated isoforms of chitinase, released during early stages of imbibition, have also been detected 329 .…”

Section: Chitinases (Pr-3)mentioning

confidence: 99%

“…Chitinases from barley seed belong to class I and II 145,181,283,329 . A barley seed chitinase, 28 kDa and pI 9.7, efficiently inhibited the growth of T. reesei, Phycomyces blakesleeanus, Alternaria alternaria and a protoplastforming mutant of Neurospora crassa 283 , while the 33 kDa chitinase, pI 9.8, inhibited the growth of T. viride, and had lysozyme activity, as measured by the lysis of cell walls of Micrococcus lysodeikticus 145 .…”

Section: Chitinases (Pr-3)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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Properties of Barley Seed Chitinases and Release of Embryo-Associated Isoforms during Early Stages of Imbibition

Cited by 74 publications

References 33 publications

Gene-Expression Patterns and Levels of Jasmonic Acid in Rice Treated with the Resistance Inducer 2,6-Dichloroisonicotinic Acid

Gene-Expression Patterns and Levels of Jasmonic Acid in Rice Treated with the Resistance Inducer 2,6-Dichloroisonicotinic Acid

Molecular Cloning and Functional Analysis of a Novel Type of Bowman-Birk Inhibitor Gene Family in Rice

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

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