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  • 1
    Electronic Resource
    Electronic Resource
    Purification of an antifungal PR-5 protein from flower buds of Brassica campestris and cloning of its gene (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 101 (1997), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: An antifungal pathogenesis-related (PR) group 5 protein with a molecular mass of 27 kDa (BFTP) was purified from flower buds of Brassica campestris. BFTP exhibits antifungal activity against Neurospora crassa, causing rapid release of cytoplasmic material at the hyphal tips of the fungus. BFTP immuno-cross-reacts with antiserum raised against the tobacco osmotin-like PR-5 protein. Using a PCR product generated with the help of two degenerate PCR primers for (1) the N-terminal amino acid sequence of the protein and (2) the conserved peptide domain that appears in all PR-5 proteins, we were able to isolate from a flower-bud cDNA library a cDNA (933 bp) that encodes this protein (pBFTP). The deduced amino acid sequence shows high similarity to PWIR2 from wheat (43%) and thaumatin II from Thaumatococcus daniellii Benth (40%). It contains the 16 cysteine residues that are conserved in all PR-5 proteins at their invariant positions. The cDNA predicts the synthesis of a preprotein which is subsequently processed into the mature protein by removal of an N-terminal signal peptide. The mRNA is predominantly expressed in flower buds, with a moderate level of transcripts detected in stems. Very low levels of the mRNA are present in root and leaf tissue. The gene is a member of a small multigene family in the genome of B. campestris.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1997.tb01041.x
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  • 2
    Electronic Resource
    Electronic Resource
    Characterization of two fungal-elicitor-induced rice cDNAs encoding functional homologues of the rab-specific GDP-dissociation inhibitor (1999)
    Springer
    Planta 210 (1999), S. 143-149 
    Details
    ISSN: 1432-2048
    Keywords: Key words: Differential display ; Functional analysis ; Fungal elicitor treatment ; Oryza (rab-GDIs) ; Pathogen signaling ; Rab-specific GDP dissociation inhibitor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. By using the mRNA differential display approach to isolate defense signaling genes active at the early stage of fungal infection two cDNA fragments with high sequence homology to rab-specific GDP-dissociation inhibitors (GDIs) were identified in rice (Oryza sativa L.) suspension cells. Using polymerase-chain-reaction products as probes, two full-length cDNA clones were isolated from a cDNA library of fungal-elicitor-treated rice, and designated as OsGDI1 and OsGDI2. The deduced amino acid sequences of the isolated cDNAs exhibited substantial homology to Arabidopsis rab-GDIs. Northern analysis revealed that transcripts detected with the 3′-gene-specific DNA probes accumulated to high levels within 30 min after treatment with a fungal elicitor derived from Magnaporthe grisea. The functionality of the OsGDIs was demonstrated by their ability to rescue the Sec19 mutant of Saccharomyces cerevisiae which is defective in vesicle transport. The proteins, expressed in Escherchia coli, cross-reacted with a polyclonal antibody prepared against bovine rab-GDI. Like bovine rab-GDI, the OsGDI proteins efficiently dissociated rab3A from bovine synaptic membranes. Using the two-hybrid system, it was shown that the OsGDIs specifically interact with the small GTP-binding proteins belonging to the rab subfamily. The specific interaction was also demonstrated in vitro by glutathione S-transferase resin pull-down assay.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004250050663
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  • 3
    Electronic Resource
    Electronic Resource
    Molecular cloning, expression, and functional characterization of a 2Cys-peroxiredoxin in Chinese cabbage (1999)
    Springer
    Plant molecular biology 40 (1999), S. 825-834 
    Details
    ISSN: 1573-5028
    Keywords: 2Cys-peroxiredoxin ; Chinese cabbage ; expression ; functional characterization ; gene cloning
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A cDNA (C2C-Prx) corresponding to a 2Cys-peroxiredoxin (2Cys-Prx) was isolated from a leaf cDNA library of Chinese cabbage. The predicted amino acid sequence of C2C-Prx has 2 conserved cysteines and several peptide domains present in most of the 2Cys-Prx subfamily members. It shows the highest sequence homology to the 2Cys-Prx enzymes of spinach (88%) and Arabidopsis (86%). Southern analysis using the cDNA insert of C2C-Prx revealed that it consists of a small multigene family in Chinese cabbage genome. RNA blot analysis showed that the gene was predominantly expressed in the leaf tissue of Chinese cabbage seedlings, but the mRNA was generally expressed in most tissues of mature plant, except roots. The expression of C2C-Prx was slightly induced by treatment with H2O2 (100μM) or Fe3+/O2/DTT oxidation system, but not by ABA (50 μM) or GA3 (10 μM). The C2C-Prx is encoded as a preprotein of 273 amino acids containing a putative chloroplast-targeting signal of 65 amino acids at its N-terminus. The N-terminally truncated recombinant protein (ΔC2C-Prx) migrates as a dimer in a non-reducing SDS-polyacrylamide gel and as a monomer in a reducing condition. The ΔC2C-Prx shows no immuno cross-reactivity to antiserum of the yeast thiol-specific antioxidant protein, and vice versa. The ΔC2C-Prx prevents the inactivation of glutamine synthetase and the DNA cleavage in the metal-catalyzed oxidation system. In the yeast thioredoxin system containing thioredoxin reductase, thioredoxin, and NADPH, the ΔC2C-Prx exhibits peroxidase activity on H2O2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006271823973
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  • 4
    Electronic Resource
    Electronic Resource
    Isolation of an additional soybean cDNA encoding Ypt/Rab-related small GTP-binding protein and its functional comparison to Sypt using a yeast ypt1-1 mutant (1996)
    Springer
    Plant molecular biology 31 (1996), S. 783-792 
    Details
    ISSN: 1573-5028
    Keywords: complementation ; small GTP-binding protein ; soybean cDNAs ; Ypt/Rab-related genes ; ypt-1 mutant
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have previously reported the isolation of a gene from a soybean cDNA library encoding a Ypt/Rab-related small GTP-binding protein, Sypt. Here, we report the isolation of a second Ypt/Rab-related gene, designated Srab2, from the same soybean cDNA library. And we compare the in vivo function of the two soybean genes utilizing a yeast ypt1-1 mutant. The Srab2 gene encodes 211 amino acid residues with a molecular mass of 23 169 Da. The deduced amino acid sequence of the Srab2 is closely related to the rat (76%) and human (75%) Rab2 proteins, but it shares relatively little homology to Sypt (46%) and Saccharomyces cerevisiae ypt proteins (41%). Genomic Southern blot analysis using the cDNA insert of Srab2 revealed that it belongs to a multigene family in the soybean genome. The protein encoded by Srab2 gene, when expressed in Escherichia coli, disclosed a GTP-binding activity. The expression pattern of the Srab2 gene is quite different from that of the Sypt gene. The Srab2 gene is predominantly expressed in the plumule region, while expression was very low in the other areas in soybean seedlings. On the other hand, the Sypt mRNA is not detectable in any tissues of soybean seedlings grown in the dark. However, light significantly suppressed the Srab2 gene expression, but enhanced the transcript levels of the Sypt gene in leaf and, at even higher levels, in root tissues. When the Srab2 and Sypt genes are introduced separately into a S cerevisiae defective in vesicular transport function, the Srab2 gene cannot complement the temperature-sensitive yeast ypt1-1 mutation at all, in contrast to the Sypt gene. In conclusion, the difference of functional complementation of the yeast mutation together with differential expression of the two genes suggest that the in vivo roles of the Srab2 and Sypt genes may be different in soybean cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00019466
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  • 5
    Electronic Resource
    Electronic Resource
    The presence of a Sar1 gene family in Brassica campestris that suppresses a yeast vesicular transport mutation Sec12-1 (1997)
    Springer
    Plant molecular biology 33 (1997), S. 1025-1035 
    Details
    ISSN: 1573-5028
    Keywords: Brassica Sar1-like cDNAs ; small GTP-binding protein ; suppression ; yeast Sec12-1 mutant
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two new members (Bsar1a and Bsar1b) of the Sar1 gene family have been identified from a flower bud cDNA library of Brassica campestris and their functional characteristics were analyzed. The two clones differ from each other at 14 positions of the 193 amino acid residues deduced from their coding region. The amino acid sequences of Bsar1a and Bsar1b are most closely related to the Sar1 family, genes that function early in the process of vesicle budding from the endoplasmic reticulum (ER). The sequences contain all the conserved motifs of the Ras superfamily (G1–G4 motifs) as well as the distinctive structural feature near the C-terminus that is Sar1 specific. Our phylogenetic analysis confirmed that these two clones can indeed be considered members of the Sar1 family and that they have a close relationship to the ARF family. The Bsar1 proteins, expressed in Escherichia coli, cross-reacted with a polyclonal antibody prepared against Saccharomyces cerevisiae Sar1 protein. It also exhibited GTP-binding activity. Genomic Southern blot analysis, using the 3'-gene-specific regions of the Bsar1 cDNAs as probes, revealed that the two cDNA clones are members of a B. campestris Sar1 family that consists of 2 to 3 genes. RNA blot analysis, using the same gene-specific probes, showed that both genes are expressed with similar patterns in most tissues of the plant, including leaf, stem, root, and flower buds. Furthermore, when we placed the two Bsar1 genes under the control of the yeast pGK1 promoter into the temperature-sensitive mutant yeast strain S. cerevisiae Sec12-1, they suppressed the mutation which consists of a defect in vesicle transport. The amino acid sequence similarity, the GTP-binding activity, and the functional suppression of the yeast mutation suggest that the Bsar1 proteins are functional homologues of the Sar1 protein in S. cerevisiae and that they may perform similar biological functions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005731209124
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