Structure and stress-related expression of two cDNAs encoding proteinase inhibitor II of Nicotiana glutinosa L.

Choi, Do Il; Park, Jong A.; Seo, Young Sam; Chun, Yoon Joo; Kim, Woo Taek

doi:10.1016/s0167-4781(00)00073-7

Cited by 32 publications

(21 citation statements)

References 18 publications

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“…There is also precedent for precursors containing repeated domains of small defenserelated proteins. The proteinase inhibitor precursors from tobacco species have up to six or eight repeated proteinase inhibitor domains (34,35) that are released after transit through the secretory pathway. Precursors with eight cysteine proteinase inhibitor domains have been identified in potato (36), and Impatiens balsamina has a precursor that is processed into six small cysteine-rich antimicrobial peptides (37).…”

Section: Discussionmentioning

confidence: 99%

Biosynthesis and insecticidal properties of plant cyclotides: The cyclic knotted proteins from Oldenlandia affinis

Jennings

West

Waine

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

469

679

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Several members of the Rubiaceae and Violaceae families produce a series of cyclotides or macrocyclic peptides of 29 -31 amino acids with an embedded cystine knot. We aim to understand the mechanism of synthesis of cyclic peptides in plants and have isolated a cDNA clone that encodes the cyclotide kalata B1 as well as three other clones for related cyclotides from the African plant Oldenlandia affinis. The cDNA clones encode prepropeptides with a 20-aa signal sequence, an N-terminal prosequence of 46 -68 amino acids and one, two, or three cyclotide domains separated by regions of about 25 aa. The corresponding cyclotides have been isolated from plant material, indicating that the cyclotide domains are excised and cyclized from all four predicted precursor proteins. The exact processing site is likely to lie on the N-terminal side of the strongly conserved GlyLeuPro or SerLeuPro sequence that flanks both sides of the cyclotide domain. Cyclotides have previously been assigned an antimicrobial function; here we describe a potent inhibitory effect on the growth and development of larvae from the Lepidopteran species Helicoverpa punctigera.

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Section: Discussionmentioning

confidence: 99%

Biosynthesis and insecticidal properties of plant cyclotides: The cyclic knotted proteins from Oldenlandia affinis

Jennings

West

Waine

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

469

679

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“…1 through 5, Wound-treated samples after 0, 0.5, 1, 4, and 12 h of culture, respectively, in Murashige and Skoog liquid medium; C, the wound-treated sample after a 4-h culture in distilled water as control. gen/plant cell wall-derived elicitors (Roby et al, 1987;Rickauer et al, 1989;Cordero et al, 1994;McGurl et al, 1995;Choi et al, 2000;Pernas et al, 2000). Furthermore, in vitro experiments showed that growth of fungi or activities of proteinases from fungi were inhibited by proteinase inhibitors (Senser et al, 1974;Mosolov et al, 1976Mosolov et al, , 1979Brown and Ryan, 1984;MacGibbon and Mann, 1986;Xie et al, 1996).…”

Section: Discussionmentioning

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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“…PI proteins of the Kunitz family were identiWed from salt-treated radish (Lopez et al 1994) and drought-stressed Arabidopsis thaliana (Gosti et al 1995). The NGP1-1 encoding Nicotiana glutinosa proteinase inhibitor II was rapidly activated by pathogen and wound-related stresses (Choi et al 2000). A cysteine-proteinase inhibitor gene from chestnut, designated CsC, was strongly induced in the roots and leaves of chestnut plantlets subjected to cold-and saline-shocks, and also in the roots after heat stress (Pernas et al 2000).…”

Section: Introductionmentioning

confidence: 99%

Characterization of a stress responsive proteinase inhibitor gene with positive effect in improving drought resistance in rice

Huang

Xiao

Xiong

2007

Planta

105

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A full-length cDNA gene, designated Oryza sativa chymotrypsin inhibitor-like 1 (OCPI1), was characterized in rice. The predicted protein of OCPI1 shows very high sequence identity to reported chymotrypsin inhibitors from various plant species. Northern-blot analysis showed that the expression of OCPI1 was strongly induced by dehydration stresses and abscisic acid (ABA). The expression of beta-glucuronidase (GUS) reporter gene under the control of OCPI1 promoter transformed into rice was strongly induced by drought and salt stresses. Interestingly, strong dehydration stress-induced GUS activity was also detected in the transgenic rice containing the reverse sequence of OCPI1 promoter fused to GUS gene, suggesting of a bidirectional transcriptional activity in the OCPI1 promoter. OCPI1 gene was over-expressed in japonica cv. Zhonghua 11 and transgenic plants containing single copy of transgene were tested for drought resistance at reproductive stage. The positive transgenic plants (OCPI1 was over-expressed) had significantly higher grain yield and seed setting rate than the wild type and the negative transgenic control (no over-expression of the transgene) under the severe drought stress conditions, whereas the potential yield of transgenic plants under normal growth conditions was not affected. Chymotrypsin-inhibitor activity assay showed that the crude protein of the positive transgenic plants had stronger inhibitory activity than the negative control. Transgenic plants had less decrease of total proteins than the wild type under drought stress. Taken together, these data indicate that OCPI1 might potentially be useful in the genetic improvement of drought resistance in rice.

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Structure and stress-related expression of two cDNAs encoding proteinase inhibitor II of Nicotiana glutinosa L.

Cited by 32 publications

References 18 publications

Biosynthesis and insecticidal properties of plant cyclotides: The cyclic knotted proteins from Oldenlandia affinis

Biosynthesis and insecticidal properties of plant cyclotides: The cyclic knotted proteins from Oldenlandia affinis

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

Characterization of a stress responsive proteinase inhibitor gene with positive effect in improving drought resistance in rice

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