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  • 1
    Electronic Resource
    Electronic Resource
    Ethylene regulation of an ERS1 homolog in mung bean seedlings (1999)
    Copenhagen : Munksgaard
    Physiologia plantarum 106 (1999), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: ETR1 (ethylene resistant) and ERS1 (ethylene response sensor) have been shown to act as a receptor for ethylene in Arabidopsis. We isolated a full length cDNA clone (VR-ERS1) encoding the ERS1 homolog from mung bean hypocotyls by screening a cDNA library with a partial cDNA fragment obtained by the reverse transcriptase-polymerase chain reaction (RT-PCR) method. VR-ERS1 is 2 477 bp long and contains a single open reading frame encoding 636 amino acids (Mr=70.9 kDa). The predicted amino acid sequence shares a high degree of identity (72–78%) with other ERS1 homologs from Arabidopsis, tomato and Rumex palustris, and is 39% identical to Arabidopsis ERS2. Genomic Southern blot analysis using a gene-specific probe suggests the existence of one copy of the VR-ERS1 gene in the mung bean genome. Northern hybridization indicates that the level of VR-ERS1 transcript varies in different parts of dark- and light-grown mung bean seedlings, with the greatest amount of the transcript being detected in apical hooks. Results showed that the abundance of the message was highly inducible by ethylene in all tissues examined. However, the magnitudes of ethylene-induction of VR-ERS1 were significantly different in each part of mung bean seedlings, with the leaf tissue being most sensitive to ethylene and there being an 8-fold increase in mRNA level after 6 h ethylene treatment. These results suggest that ethylene positively modulates the expression of its receptor gene in the vegetative tissues of mung bean plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.1999.106113.x
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  • 2
    Electronic Resource
    Electronic Resource
    Temporal and spatial regulation of the expression of 1-aminocyclopropane-1-carboxylate oxidase by ethylene in mung bean (Vigna radiata) (1999)
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 105 (1999), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Ethylene induced an increase in the level of 1-aminocyclopropane-1-carboxylate oxidase (VR-ACO1) transcript in mung bean hypocotyls. Time course study revealed that the level of the VR-ACO1 mRNA in excised mung bean hypocotyls increased after 2-h ethylene treatment and much higher mRNA levels were observed thereafter, while the basal level of transcript was slightly decreased in control tissues. The in vivo ACC oxidase activity increased from 31 nl g−1 h−1 at zero time to maximum activity of 62 nl g−1 h−1 at 10-h ethylene treatment. Polyclonal antibody against VR-ACO1 protein expressed in E. coli cells was generated. Immunoblot analysis using the resulting antiserum showed that the induction pattern of ACC oxidase polypeptide was in parallel with that of enzyme activity during the incubation with ethylene. Thus, ethylene increases the levels of the VR-ACO1 mRNA and ACC oxidase protein as well as enzyme activity in mung bean hypocotyls. The abundance of the VR-ACO1 transcript and protein was also induced in all parts of light-grown mung bean seedlings by ethylene treatment. However, both the basal levels and the magnitudes of ethylene-induction of VR-ACO1 were markedly different in different tissues, with the roots being the most sensitive to ethylene. These results suggest that the different part of mung bean seedlings has a distinct potential to respond to ethylene with regard to ACC oxidase gene activation. Furthermore, our data suggest that the induction of VR-ACO1 by ethylene is subject not only to transcriptional control but also to posttranscriptional control in hypocotyls, whereas ethylene regulates the VR-ACO1 gene expression mainly at the transcriptional level in roots. The possible molecular mechanism of regulation of ACC oxidase gene expression by ethylene and its significance are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.1999.105120.x
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  • 3
    Electronic Resource
    Electronic Resource
    Formation of wheat protein bodies: Involvement of the Golgi apparatus in gliadin transport (1988)
    Springer
    Planta 176 (1988), S. 173-182 
    Details
    ISSN: 1432-2048
    Keywords: Gliadin ; Golgi apparatus ; Protein deposition ; Storage protein ; Triticum (protein bodies)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Developing wheat (Triticum aestivum L.) endosperm was examined using ultrathin sections prepared from tissues harvested at 5, 9, 16 and 25 d after flowering. Protein bodies were evident by 9 d and displayed a variety of membranous structures and inclusions. The Golgi apparatus was a prominent organelle at all stages, and by 9 d was associated with small electron-dense inclusions. By immunocytochemical techniques, gliadin (wheat prolamine) was localized within these vesicles and in homogeneous regions of protein bodies, but not in the lumen of the rough endoplasmic reticulum. The protein bodies appear to enlarge by fusion of smaller protein bodies resulting in larger, irregular-shaped organelles. The affinity of the Golgi-derived vesicles for gliadin-specific probes during the period of maximal storage-protein synthesis and deposition indicates that this organelle includes the bulk, if not all, of the gliadin produced. The involvement of the Golgi apparatus in the packaging of gliadins into protein bodies indicates a pathway which differs from the mode of prolamine deposition in other cereals such as maize, rice and sorghum, and resembles the mechanism employed for the storage of rice glutelin and legume globulins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00392442
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  • 4
    Electronic Resource
    Electronic Resource
    Structure and expression of cDNAs encoding 1-aminocyclopropane-1-carboxylate oxidase homologs isolated from excised mung bean hypocotyls (1994)
    Springer
    Planta 194 (1994), S. 223-229 
    Details
    ISSN: 1432-2048
    Keywords: 1-Aminocyclopropane-1-carboxylate oxidase ; Ethylene ; Gene expression ; Hypocotyl excision ; Vigna ; Wounding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract By screening a mung bean (Vigna radiata L.) hypocotyl cDNA library using a combination of apple (pAE12) and tomato (pTOM13) 1-aminocyclopropane1-carboxylate (ACC)-oxidase cDNAs as probes, putative ACC-oxidase clones were isolated. Based on restriction-enzyme map and DNA-sequencing analyses, they can be divided into two homology classes, represented by pVR-ACO1 and pVR-ACO2. While pVR-ACO1 and pVR-ACO2 exhibit close homology in their coding regions, their 3′-noncoding regions are divergent. pVR-ACO1 is a 1312-bp full-length clone and contains a single open reading frame encoding 317 amino acids (MW = 35.8 kDa), while pVR-ACO2 is 1172 bp long and is a partial cDNA clone encoding 308 amino acids. These two deduced amino-acid sequences share 83% identity, and display considerable sequence conservation (73–86%) to other ACC oxidases from various plant species. Northern blot analyses of RNAs isolated from hypocotyl, leaf, and stem tissues using gene-specific probes indicate that the pVR-ACO1 transcript is present in all parts of the seedling and that the expression in hypocotyls is further increased following excision. The maximum induction of ACC-oxidase transcripts occurred at about 6 h after excision, while the maximum enzyme activity was observed at 24 h. When excised hypocotyls were treated with ethylene a further enhanced level of transcripts was observed. Aminooxyacetic acid, an inhibitor of ACC-synthase activity, and 2,5-norbornadiene, an inhibitor of ethylene action, suppressed the wound-induced accumulation of ACC-oxidase mRNA, while an addition of ethylene in these tissues restored the accumulation of ACC-oxidase mRNA. These results indicate that the wound-induced expression of ACC-oxidase transcripts is mediated through wound-induced ethylene. Furthermore, when intact mung-bean seedlings were treated with exogenous ethylene, a marked increase in the level of ACC-oxidase mRNA was observed. Together, these results indicate that ethylene plays a key role in activating the expression of the ACC-oxidase gene in both intact and excised mung-bean hypocotyls.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00196391
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  • 5
    Electronic Resource
    Electronic Resource
    Structure and expression of cDNAs encoding 1-aminocyclopropane-1-carboxylate oxidase homologs isolated from excised mung bean hypocotyls (1994)
    Springer
    Planta 194 (1994), S. 223-229 
    Details
    ISSN: 1432-2048
    Keywords: 1-Aminocyclopropane-1-carboxylate oxidase ; Ethylene ; Gene expression ; Hypocotyl excision ; Vigna ; Wounding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract By screening a mung bean (Vigna radiata L.) hypocotyl cDNA library using a combination of apple (pAE12) and tomato (pTOM13) 1-aminocyclopropane1-carboxylate (ACC)-oxidase cDNAs as probes, putative ACC-oxidase clones were isolated. Based on restriction-enzyme map and DNA-sequencing analyses, they can be divided into two homology classes, represented by pVR-ACO1 and pVR-ACO2. While pVR-ACO1 and pVR-ACO2 exhibit close homology in their coding regions, their 3′-noncoding regions are divergent. pVR-ACO1 is a 1312-bp full-length clone and contains a single open reading frame encoding 317 amino acids (MW = 35.8 kDa), while pVR-ACO2 is 1172 bp long and is a partial cDNA clone encoding 308 amino acids. These two deduced amino-acid sequences share 83% identity, and display considerable sequence conservation (73–86%) to other ACC oxidases from various plant species. Northern blot analyses of RNAs isolated from hypocotyl, leaf, and stem tissues using gene-specific probes indicate that the pVR-ACO1 transcript is present in all parts of the seedling and that the expression in hypocotyls is further increased following excision. The maximum induction of ACC-oxidase transcripts occurred at about 6 h after excision, while the maximum enzyme activity was observed at 24 h. When excised hypocotyls were treated with ethylene a further enhanced level of transcripts was observed. Aminooxyacetic acid, an inhibitor of ACC-synthase activity, and 2,5-norbornadiene, an inhibitor of ethylene action, suppressed the wound-induced accumulation of ACC-oxidase mRNA, while an addition of ethylene in these tissues restored the accumulation of ACC-oxidase mRNA. These results indicate that the wound-induced expression of ACC-oxidase transcripts is mediated through wound-induced ethylene. Furthermore, when intact mung-bean seedlings were treated with exogenous ethylene, a marked increase in the level of ACC-oxidase mRNA was observed. Together, these results indicate that ethylene plays a key role in activating the expression of the ACC-oxidase gene in both intact and excised mung-bean hypocotyls.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01101681
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  • 6
    Electronic Resource
    Electronic Resource
    Cloning of a cDNA encoding 1-aminocyclopropane-1-carboxylate synthase and expression of its mRNA in ripening apple fruit (1991)
    Springer
    Planta 185 (1991), S. 38-45 
    Details
    ISSN: 1432-2048
    Keywords: 1-Amninocyclopropane-1-carboxylate synthase ; cDNA ; Ethylene synthesis ; Fruit ripening ; Gene expression ; Malus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract 1-Aminocyclopropane-1-carboxylate (ACC) synthase (EC 4.4.1.14) purified from apple (Malus sylvestris Mill.) fruit was subjected to trypsin digestion. Following separation by reversed-phase high-pressure liquid chromatography, ten tryptic peptides were sequenced. Based on the sequences of three tryptic peptides, three sets of mixed oligonucleotide probes were synthesized and used to screen a plasmid cDNA library prepared from poly(A)+ RNA of ripe apple fruit. A 1.5-kb (kilobase) cDNA clone which hybridized to all three probes were isolated. The clone contained an open reading frame of 1214 base pairs (bp) encoding a sequence of 404 amino acids. While the polyadenine tail at the 3′-end was intact, it lacked a portion of sequence at the 5′-end. Using the RNA-based polymerase chain reaction, an additional sequence of 148 bp was obtained at the 5′-end. Thus, 1362 bp were sequenced and they encode 454 amino acids. The deduced amino-acid sequence contained peptide sequences corresponding to all ten tryptic fragments, confirming the identity of the cDNA clone. Comparison of the deduced amino-acid sequence between ACC synthase from apple fruit and those from tomato (Lycopersicon esculentum Mill.) and winter squash (Cucurbita maxima Duch.) fruits demonstrated the presence of seven highly conserved regions, including the previously identified region for the active site. The size of the translation product of ACC-synthase mRNA was similar to that of the mature protein on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), indicating that apple ACC-synthase undergoes only minor, if any, post-translational proteolytic processing. Analysis of ACC-synthase mRNA by in-vitro translation-immunoprecipitation, and by Northern blotting indicates that the ACC-synthase mRNA was undetectable in unripe fruit, but was accumulated massively during the ripening proccess. These data demonstrate that the expression of the ACC-synthase gene is developmentally regulated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00194512
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  • 7
    Electronic Resource
    Electronic Resource
    Auxin and brassinosteroid differentially regulate the expression of three members of the 1-aminocyclopropane-1-carboxylate synthase gene family in mung bean (Vigna radiata L.) (1999)
    Springer
    Plant molecular biology 41 (1999), S. 443-454 
    Details
    ISSN: 1573-5028
    Keywords: 1-aminocyclopropane-1-carboxylate synthase ; auxin ; brassinosteroid ; ethylene ; gene expression ; hypocotyl ; promoter ; transgenic tobacco ; Vigna radiata
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Indole-3-acetic acid (IAA) markedly increased ethylene production by inducing the expression of three 1-aminocyclopropane-1-carboxylate (ACC) synthase cDNAs (pVR-ACS1, pVR-ACS6 and pVR-ACS7) in mung bean hypocotyls. Results from nuclear run-on transcription assay and RNA gel blot studies revealed that all three genes were transcriptionally active displaying unique patterns of induction by IAA and various hormones in etiolated hypocotyls. Particularly, 24-epibrassinolide (BR), an active brassinosteroid, specifically enhanced the expression of VR-ACS7 by a distinct temporal induction mechanism compared to that of IAA. In addition, BR synergistically increased the IAA-induced VR-ACS6 and VR-ACS7 transcript levels, while it effectively abolished both the IAA- and kinetin-induced accumulation of VR-ACS1 mRNA. In light-grown plants, VR-ACS1 was induced by IAA in roots, and VR-ACS6 in epicotyls. IAA- and BR-treatments were not able to increase the VR-ACS7 transcript in the light-grown tissues. These results indicate that the expression of ACC synthase multigene family is regulated by complex hormonal and developmental networks in a gene- and tissue-specific manner in mung bean plants. The VR-ACS7 gene was isolated, and chimeric fusion between the 2.4 kb 5′-upstream region and the β-glucuronidase (GUS) reporter gene was constructed and introduced into Nicotiana tabacum. Analysis of transgenic tobacco plants revealed the VR-ACS7 promoter-driven GUS activity at a highly localized region of the hypocotyl-root junction of control seedlings, while a marked induction of GUS activity was detected only in the hypocotyl region of the IAA-treated transgenic seedlings where rapid cell elongation occurs. Although there was a modest synergistic effect of BR on the IAA-induced GUS activity, BR alone failed to increase the GUS activity, suggesting that induction of VR-ACS7 occurs via separate signaling pathways in response to IAA and BR. A scheme of the multiple regulatory pathways for the expression of ACC synthase multigene family by auxin and BR is presented.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006372612574
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  • 8
    Electronic Resource
    Electronic Resource
    Rice proteins that bind single-stranded G-rich telomere DNA (1998)
    Springer
    Plant molecular biology 36 (1998), S. 661-672 
    Details
    ISSN: 1573-5028
    Keywords: rice ; telomere binding protein ; single-stranded DNA binding protein ; telomerase ; telomere
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In this work, we have identified and characterized proteins in rice nuclear extracts that specifically bind the single-stranded G-rich telomere sequence. Three types of specific DNA-protein complexes (I, II, and III) were identified by gel retardation assays using synthetic telomere substrates consisting of two or more single-stranded TTTAGGG repeats and rice nuclear extracts. Since each complex has a unique biochemical property and differs in electrophoretic mobility, at least three different proteins interact with the G-rich telomere sequences. These proteins are called rice G-rich telomere binding protein (RGBP) and none of them show binding affinity to double-stranded telomere repeats or single-stranded C-rich sequence. Changing one or two G's to C's in the TTTAGGG repeats abolishes binding activity. RGBPs have a greatly reduced affinity for human and Tetrahymena telomeric sequence and do not efficiently bind the cognate G-rich telomere RNA sequence UUUAGGG. Like other telomere binding proteins, RGBPs are resistant to high salt concentrations. RNase sensitivity of the DNA-protein interactions was tested to investigate whether an RNA component mediates the telomeric DNA-protein interaction. In this assay, we observed a novel complex (complex III) in gel retardation assays which did not alter the mobilities or the band intensities of the two pre-existing complexes (I and II). The complex III, in addition to binding to telomeric sequences, has a binding affinity to rice nuclear RNA, whereas two other complexes have a binding affinity to only single-stranded G-rich telomere DNA. Taken together, these studies suggest that RGBPs are new types of telomere-binding proteins that bind in vitro to single-stranded G-rich telomere DNA in the angiosperms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005994719175
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