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At least 19 recordsLinked to original sources
PubMed1986

Metabolism of gibberellin a(12)-7-aldehyde by soybean cotyledons and its use in identifying gibberellin a(7) as an endogenous gibberellin.

The level of gibberellin(GA)-like material in cotyledons of soybean (Glycine max L.) was highest at mid-pod fill-about 10 nanograms GA(3) equivalents per gram fresh weight of tissue, assayed in the immersion dwarf rice bioassay. This amount is about 1000-fold less than levels in Pisum and Phaseolus seed, other legume species whose spectrum of endogenous gibberellins (GAs) is well known. The metabolism of [(14)C]-GA(12)-7-aldehyde (GA(12)ald)-the universal GA precursor-by intact, mid-pod-fill, soybean cotyledons and their cell-free extracts was investigated. In 4 hours, extracts converted GA(12)ald to two products-[(14)C]GA(12) (42% yield) and [(14)C]GA(15) (7%). Within 5 minutes, intact embryos converted GA(12)ald to [(14)C]GA(12) and [(14)C]GA(15) in 15% yield; 4 hour incubations afforded at least 22 products (96% total yield). The putative [(14)C]GA(12) was identified as a product of [(14)C]GA(12)ald metabolism on the basis of co-chromatography with authentic GA(12) on a series of reversed and normal phase high pressure liquid chromatography (HPLC) and thin-layer chromatography (TLC) systems, and by a dual feed of the putative [(14)C]GA(12) and authentic [(14)C]GA(12) to cotyledons of both peas and soybeans. The [(14)C]GA(15) was identified as a metabolite of [(14)C]GA(12)ald by capillary gas chromatography (GC)-mass-spectrometry-selected ion monitoring, GC-radiocounting, HPLC, and TLC. By adding the [(14)C] metabolites of [(14)C]GA(12)ald to a different and larger extract (about 0.2 kg fresh weight of soybean reproductive tissue) and purifying endogenous substances co-chromatographing with these metabolites, at least two GA-like substances were obtained and one identified as GA(7) by GC-mass spectrometry. Since [(14)C]GA(9) was not found as a [(14)C]metabolite of [(14)C]GA(12)ald, soybean embryos might have a pathway for biosynthesis of active, C-19 gibberellins like that of the cucurbits; GA(12)ald --> GA(12) --> GA(15) --> GA(24) --> GA(36) --> GA(4) --> GA(7).

Journal Article↗
PubMed1987

Gibberellins and gravitropism in maize shoots: endogenous gibberellin-like substances and movement and metabolism of [3H]Gibberellin A20.

[3H]Gibberellin A20 (GA20) of high specific radioactivity (49.9 gigabecquerel per millimole) was applied equilaterally in a ring of microdrops to the internodal pulvinus of shoots of 3-week-old gravistimulated and vertical normal maize (Zea mays L.), and to a pleiogravitropic (prostrate) maize mutant, lazy (la). All plants converted the [3H]GA20 to [3H]GA1- and [3H]GA29-like metabolites as well as to several metabolites with the partitioning and chromatographic behavior of glucosyl conjugates of [3H]GA1, [3H]GA29, and [3H]GA8. The tentative identification of these putative [3H]GA glucosyl conjugates was further supported by the release of the free [3H]GA moiety after cleavage with cellulase. Within 12 hours of the [3H]GA20 feed, there was a significantly higher proportion of total radioactivity in lower than in upper halves of internode and leaf sheath pulvini in gravistimulated normal maize. Further, there was a significantly higher proportion of putative free GA metabolites of [3H]GA20, especially [3H]GA1, in the lower halves of normal maize relative to upper halves. The differential localization of the metabolites between upper and lower halves was not apparent in the pleiogravitropic mutant, la. Endogenous GA-like substances were also examined in gravistimulated maize shoots. Forty-eight hours after gravistimulation of 3-week-old maize seedlings, endogenous free GA-like substances in upper and lower leaf sheath and internode pulvini halves were extracted, chromatographed, and bioassayed using the "Tanginbozu" dwarf rice microdrop assay. Lower halves contained consistently higher total levels of GA-like activity. The qualitative elution profile of GA-like substances differed consistently, upper halves containing principally a GA20-like substance and lower halves containing principally a GA20-like substance and lower halves containing mainly GA1-like and GA19-like substances. Gibberellins A1 (10 nanograms per gram) and A20 (5 nanograms per gram) were identified from these lower leaf sheath pulvini by capillary gas chromatography-selected ion monitoring. Results from all of these experiments are consistent with a role for GAs in the differential shoot growth that follows gravitropism, although the results do not eliminate the possibility that the redistribution of GAs results from the gravitropic response.

Gibberellins↗
PubMed1996

Gibberellin Metabolism in Maize (The Stepwise Conversion of Gibberellin A12-Aldehyde to Gibberellin A20.

The stepwise metabolism of gibberellin A12-aldehyde (GA12-aldehyde) to GA20 is demonstrated from seedling shoots of maize (Zea mays L.). The labeled substrates [13C,3H]GA12-aldehyde, [13C,3H]GA12, [14C4]GA53, [14C4/2H2]GA44, and [14C4/2H2]GA19 were fed individually to dwarf-5 vegetative shoots. Both [13C,3H]GA12-aldehyde and [13C,3H]GA12 were also added individually to normal shoots. The labeled metabolites were identified by full-scan gas chromatography-mass spectrometry and Kovats retention indices. GA12-aldehyde was metabolized to GA53-aldehyde, GA12, GA53, GA44, and GA19; GA12 was metabolized to 2[beta]-hydroxy-GA12, GA53, 2[beta]-hydroxyGA53, GA44, 2[beta]-hydroxyGA44, and GA19; GA53 was metabolized to GA44, GA19, GA20, and GA1; GA44 was metabolized to GA19; and GA19 was metabolized to GA20. These results, together with previously published data from this laboratory, document the most completely defined gibberellin pathway for the vegetative tissues of higher plants.

Journal Article↗
PubMed2000

Gibberellin-induced changes in growth anisotropy precede gibberellin-dependent changes in cortical microtubule orientation in developing epidermal cells of barley leaves. Kinematic and cytological studies on a gibberellin-responsive dwarf mutant, M489.

We conducted kinematic and cytological studies on "between vein" epidermal cells of the gibberellin (GA)-deficient M489 dwarf mutant of barley (Hordeum vulgare L. Himalaya). GAs affect radial and axial components of cell expansion and cortical microtubule orientation. Adaxial cells in particular expand radially after leaving the elongation zone (EZ), probably as part of leaf unrolling. Exogenous gibberellic acid corrects the mutant's short, wide blades, short EZ, and slow elongation rate. Cell production rates increase more on the adaxial than on the abaxial surface. Cells spend equal periods of time elongating in dwarf and tall plants, but relative elemental growth rates start to decline sooner in the dwarf. GA increased the rate at which longitudinal wall area increased because the increased axial growth more than compensated for reduced radial growth. In dwarf leaves, increased radial expansion was detected in basal parts of the EZ before cortical microtubules lost transverse orientation in the distal elongation zone. We conclude that loss of microtubule orientation is not required for low GA levels to reduce growth anisotropy.

Gibberellins↗
PubMed1975

Metabolism of Tritiated Gibberellins in d-5 Dward Maize: II. [H]Gibberellin A(1), [H]Gibberellin A(3), and Related Compounds.

After 30 minutes of incubation of young leaf sections of d-5 maize (Zea mays L.) in [(3)H]gibberellin A(1) ([(3)H]GA(1)), the metabolite [(3)H]GA(8) was present in significant amounts, with a second metabolite, [(3)H]GA(8)-glucose ([(3)H]GA(8)-glu), appearing soon after. A third [(3)H]GA(1) metabolite, the polar uncharacterized conjugate [(3)H]GA(1)-X, took more than 1 hour to appear. The protein synthesis inhibitor cycloheximide inhibited the production of all [(3)H]GA(1) metabolites, indicating a possible protein synthesis requirement for [(3)H]GA(1) metabolism.By preincubating leaf sections in unlabeled GA(1) before exposure to [(3)H]GA(1) or by reducing the specific radioactivity of the [(3)H]GA(1) supplied, it was possible to reduce greatly the conversion of radioactive GA(1) to [(3)H]GA(8)-glu, without affecting conversion to [(3)H]GA(1)-X. Increasing the molar concentration of the [(3)H]GA(1) fed greatly increased the molar yield of [(3)H]GA(1)-X, whereas the molar yields of [(3)H]GA(8) and [(3)H]GA(8)-glu were much less affected.The principal metabolite of [(3)H]GA(3) was a very polar compound having chromatographic properties similar to those of the conjugate [(3)H]GA(1)-X produced from [(3)H]GA(1). The naturally occurring GAs [(3)H]GA(1), [(3)H]GA(3), and [(3)H]tetrahydroGA(3) were metabolized to a much greater extent than were the artifical derivatives [(3)H]ketoGA(1), [(3)H]GA(1)-methyl ester, and [(3)H]pseudoGA(1). Only [(3)H]GA(1) and [(3)H]GA(3), with their identical D ring structures, were converted to [(3)H]GA(1)-X type compounds; [(3)H]-ketoGA(1) and [(3)H]tetrahydroGA(3), with modified D rings, were not converted to this type of conjugate.

Journal Article↗
PubMed1990

Gibberellin A(3) Is Biosynthesized from Gibberellin A(20) via Gibberellin A(5) in Shoots of Zea mays L.

[17-(13)C,(3)H]-Labeled gibberellin A(20) (GA(20)), GA(5), and GA(1) were fed to homozygous normal (+/+), heterozygous dominant dwarf (D8/+), and homozygous dominant dwarf (D8/D8) seedlings of Zea mays L. (maize). (13)C-Labeled GA(29), GA(8), GA(5), GA(1), and 3-epi-GA(1), as well as unmetabolized [(13)C]GA(20), were identified by gas chromatography-selected ion monitoring (GC-SIM) from feeds of [17-(13)C, (3)H]GA(20) to all three genotypes. (13)C-Labeled GA(8) and 3-epi-G(1), as well as unmetabolized [(13)C]GA(1), were identified by GC-SIM from feeds of [17-(13)C, (3)H]GA(1) to all three genotypes. From feeds of [17-(13)C, (3)H]GA(5), (13)C-labeled GA(3) and the GA(3)-isolactone, as well as unmetabolized [(13)C]GA(5), were identified by GC-SIM from +/+ and D8/D8, and by full scan GC-MS from D8/+. No evidence was found for the metabolism of [17-(13)C, (3)H]GA(5) to [(13)C]GA(1), either by full scan GC-mass spectrometry or by GC-SIM. The results demonstrate the presence in maize seedlings of three separate branches from GA(20), as follows: (a) GA(20) --> GA(1) --> GA(8); (b) GA(20) --> GA(5) --> GA(3); and (c) GA(20) --> GA(29). The in vivo biogenesis of GA(3) from GA(5), as well as the origin of GA(5) from GA(20), are conclusively established for the first time in a higher plant (maize shoots).

Journal Article↗
PubMed2005

Similarities and differences between the characteristics of gibberellin-binding protein and gibberellin 2-oxidases in adzuki bean (Vigna angularis) seedlings.

Gibberellin-binding proteins (GBPs) were purified ca. 230,000 fold. The characteristics of adzuki GBP were examined and compared with those of a recombinant gibberellin 2-oxidase (rVaGA2oxA1) that was fused with glutathione S-transferase (GST). VaGA2oxA1 was most abundantly expressed in etiolated adzuki bean seedlings, and VaGA2oxA1 and GBPs from adzuki bean seedlings showed gibberellin-binding activity when incubated with 2-oxoglutarate and Co2+. Both rVaGA2oxA1 and partially purified GBPs from adzuki bean seedlings showed very similar selectivity to gibberellins in binding assays, where biologically active gibberellins such as GA4, GA3, GA7, and GA1 showed higher binding affinity than biologically inactive gibberellins such as GA8, GA34, and 3-epi-GA4. The polyclonal antibody raised against rVaGA2oxA1 cross-reacted with all rVaGA2oxs (rVaGA2oxA1, rVaGA2oxA2, rVaGA2oxB1, rVaGA2oxB2, and rVaGA2oxB3) whose cDNAs were cloned from adzuki bean seedlings. Treated with the antibody, the recombinants that originally showed gibberellin-binding activity lost both binding activity and enzymatic activity. In contrast to the recombinants, the gibberellin-binding activity of GBPs from adzuki bean seedlings was hardly affected by the antibody treatment. The GBPs showed very weak gibberellin 2-oxidase-like activity, and it was not affected by the antibody treatment either. These observations suggest that a major component that showed GA-binding activity was apparently different from any gibberellin 2-oxidase cloned from the seedlings.

Carrier Proteins↗
PubMed2004

Two rice GRAS family genes responsive to N -acetylchitooligosaccharide elicitor are induced by phytoactive gibberellins: evidence for cross-talk between elicitor and gibberellin signaling in rice cells.

In this study, we present data showing that two members of the GRAS family of genes from rice, CIGR1 and CIGR2 (chitin-inducible gibberellin-responsive), inducible by the potent elicitor N -acetylchitooligosaccharide (GN), are rapidly induced by exogenous gibberellins. The pattern of mRNA accumulation was dependent on the dose and biological activity of the gibberellins, suggesting that the induction of the genes by gibberellin is mediated by a biological receptor capable of specific recognition and signal transduction upon perception of the phytoactive compounds. Further pharmacological analysis revealed that the CIGR1 and CIGR2 mRNA accumulation by treatment with gibberellin is dependent upon protein phosphorylation/dephosphorylation events. In rice calli derived from slender rice 1, a constitutive gibberellin-responsive mutant, or d1, a mutant deficient in the alpha -subunit of the heterotrimeric G-protein, CIGR1 and CIGR2 were induced by a GN elicitor, yet not by gibberellin. Neither gibberellin nor GN showed related activities in defense or development, respectively. These results strongly suggested that the signal transduction cascade from gibberellin is independent of that from GN, and further implied that CIGR1 and CIGR2 have dual, distinct roles in defense and development.

Blotting, Northern↗
PubMed1977

Biosynthesis of gibberellins in Gibberella fujikuroi. Gibberellin A47.

Two minor radioactive products in cultures of G. fujikuroi strain ACC917 supplemented with labeled gibberellin A4 have been identified as the 2alpha-hydroxy derivative, gibberellin A47, and the hydrate, gibberellin A2. In addition, evidence was obtained by combined gas chromatography--mass spectrometry for the formation of 3-O-acetylgibberellin A1,3-O-acetylgibberellin A3, and gibberellin A20 by the culture. The time course of gibberellin synthesis in defined and complex media, as well as changes in the relative amounts of radioactive gibberellins formed when [4C]gibberellin A4 was added to cultures at different ages, suggest that the composition of the gibberellin mixture produced is determined by the balance between synthesis and decay of key enzymes in the branching pathway.

Gibberella↗
PubMed1992

Gibberellins and the Legume-Rhizobium Symbiosis : I. Endogenous Gibberellins of Lima Bean (Phaseolus lunatus L.) Stems and Nodules.

The content of gibberellin-like substances in nodules formed by Bradyrhizobium species strain 127E14 on roots of lima bean (Phaseolus lunatus L.) has been previously found to be relatively high. The objectives of the present study were to purify and identify the endogenous gibberellins from the stems and nodules of lima bean. By sequential silica gel partition column chromatography, C(18) reverse-phase high performance liquid chromatography, and combined gas chromatography-mass spectrometry, the gibberellins A(1), A(3), A(19), A(20), A(29), and A(44) were identified from root nodules. Gibberellins A(1), A(3), A(19), A(20), and A(44) were also identified from lima bean stem tissue. These data provide the first mass spectral-based evidence that gibberellins are present in leguminous root nodules. The presence of the gibberellins identified indicates that the early 13-hydroxylation gibberellin biosynthetic pathway predominates in stem and nodule tissue. However, it is not known if the gibberellins within the nodules are produced in situ, or if they are imported from some remote host plant tissue.

Journal Article↗
PubMed2001

HOW GIBBERELLIN REGULATES PLANT GROWTH AND DEVELOPMENT: A Molecular Genetic Analysis of Gibberellin Signaling.

Gibberellins are hormones that control growth and a wide variety of other plant developmental processes. In recent years, significant progress has been made on the biochemistry of gibberellin biosynthesis and on the mechanisms by which gibberellin levels are regulated in plants. There have also been major advances in the understanding of gibberellin signaling, with several key genes being cloned. This review discusses our current understanding of gibberellin signaling, as seen from the perspective of molecular genetic analysis, and relates these observations to previous biochemical studies. In particular, we highlight an important conclusion of recent years: that GAI/RGA and orthologs play major roles in gibberellin signaling in diverse plant species, and that gibberellin probably stimulates growth by derepression of GAI/RGA.

Journal Article↗
PubMed1993

Gibberellin treatment stimulates nuclear factor binding to the gibberellin response complex in a barley alpha-amylase promoter.

The promoters of a majority of cereal alpha-amylase genes contain three highly conserved sequences (gibberellin response element, box I, and pyrimidine box). Recent studies have demonstrated the functional importance of four regions that either coincide with or are immediately proximal to these three conserved elements as well as an upstream Opaque-2 binding sequence. In this study, we describe the characterization of nuclear protein factors from barley aleurone layers whose binding activity toward gibberellin response complex sequences from the barley low-pl alpha-amylase gene (Amy32b) promoter is stimulated by gibberellin A3 (GA3) treatment. Barley proteins isolated from crude nuclear extracts prepared from aleurone layers incubated with or without GA3 were fractionated by anion exchange fast protein liquid chromatography and studied using band shift assays, sequence-specific competitions, and DNase I footprinting. A GA3-dependent binding activity eluting at 210 mM KCl was shown to bind specifically to the gibberellin response element and the closely associated box I. DNase I footprinting with the proteins in this fraction indicated interactions with sequences in the gibberellin response element and box I. A second DNA binding activity eluting at 310 mM KCl was present constitutively in extracts prepared from tissues incubated both in the absence and in the presence of hormone. Proteins in this fraction were able to bind to many DNA sequences and, in general, were largely nonspecific. DNase I footprinting with the proteins in this fraction indicated a large area of protection with a single unoccupied region located at the 3' end of box I. The possible function of such an activity in hormone regulation of the alpha-amylase genes is discussed.

Base Sequence↗
PubMed1981

Characterization of a Gibberellin-Insensitive Dwarf Wheat, D6899 : EVIDENCE FOR A REGULATORY STEP COMMON TO MANY DIVERSE RESPONSES TO GIBBERELLINS.

The effects of gibberellin in two wheat varieties, Nainari 60 and D6899, have been studied. D6899 is a dwarf wheat having a single locus mutation, the Rht 3 gene ("Tom Thumb" gene), which is located on chromosome 4A. When compared with the standard height wheat variety, Nainari 60, D6899 does not have a slowdown in cellular metabolism such as respiration rate, protein content, rate of protein synthesis, and uptake of amino acids. The content of ATP is even higher in D6899. However, all of the gibberellin-mediated physiological processes that we have studied, including leaf elongation, synthesis and release of hydrolytic enzymes, and secretion of phosphate ions and reducing sugars in aleurone layers, are retarded in D6899. D6899 and Nainari 60 have essentially the same uptake and metabolism of gibberellin and their levels of endogenous inhibitors such as abscisic acid do not differ drastically. The dosage-response curve of the gibberellin-mediated alpha-amylase production indicates that a rate-limiting step, which is common to many of the diverse gibberellin responses, is partially blocked in D6899 wheat.

Journal Article↗
PubMed1987

Gibberellin Structure-Dependent Interaction between Gibberellins and Deoxygibberellin C in the Growth of Dwarf Maize Seedlings.

The effects of 3-deoxygibberellin C (DGC) on the growth-promoting actions of gibberellins A(1), A(2), A(3), A(4), A(5), A(7), A(8), A(9), A(13), A(18), A(19), A(20), and A(23) (GAn) as well as 13-deoxygibberellin A(5) (deoxy-GA(5)) were tested with seedlings of gibberellin-deficient dwarf mutants (d(2) and d(5)) of maize (Zea mays L.). It was found that DGC promoted the actions of gibberellins having both C-1 double bond and C-3 axial hydroxyl group, and it inhibited the action of gibberellins having the saturated ring A and lacking the C-3 axial hydroxyl group, whereas it did not affect that of the ones having the hydroxyl group. The presence of C-2 double bond, as in GA(5) and deoxy-GA(5), diminished the inhibitory action of DGC. The DGC inhibition was alleviated by raising the doses of the relevant GAs, suggesting that it is a competitive inhibition. These results and the finding that the growth of normal maize and rice seedlings are inhibited by DGC indicate that GA(9), GA(19), GA(20) or other gibberellins having ring A of the same structure are involved in the growth of these plants as active form(s) or as intermediate(s) leading to the active form(s).

Journal Article↗
PubMed2005

Analysis of the rice mutant dwarf and gladius leaf 1. Aberrant katanin-mediated microtubule organization causes up-regulation of gibberellin biosynthetic genes independently of gibberellin signaling.

Molecular genetic studies of plant dwarf mutants have indicated that gibberellin (GA) and brassinosteroid (BR) are two major factors that determine plant height; dwarf mutants that are caused by other defects are relatively rare, especially in monocot species. Here, we report a rice (Oryza sativa) dwarf mutant, dwarf and gladius leaf 1 (dgl1), which exhibits only minimal response to GA and BR. In addition to the dwarf phenotype, dgl1 produces leaves with abnormally rounded tip regions. Positional cloning of DGL1 revealed that it encodes a 60-kD microtubule-severing katanin-like protein. The protein was found to be important in cell elongation and division, based on the observed cell phenotypes. GA biosynthetic genes are up-regulated in dgl1, but the expression of BR biosynthetic genes is not enhanced. The enhanced expression of GA biosynthetic genes in dgl1 is not caused by inappropriate GA signaling because the expression of these genes was repressed by GA3 treatment, and degradation of the rice DELLA protein SLR1 was triggered by GA3 in this mutant. Instead, aberrant microtubule organization caused by the loss of the microtubule-severing function of DGL1 may result in enhanced expression of GA biosynthetic genes in that enhanced expression was also observed in a BR-deficient mutant with aberrant microtubule organization. These results suggest that the function of DGL1 is important for cell and organ elongation in rice, and aberrant DGL1-mediated microtubule organization causes up-regulation of gibberellin biosynthetic genes independently of gibberellin signaling.

Chromosome Mapping↗
PubMed2005

Gibberellin 2-oxidases from seedlings of adzuki bean (Vigna angularis) show high gibberellin-binding activity in the presence of 2-oxoglutarate and Co2+.

Five full-length cDNA encoding gibberellin 2-oxidases, VaGA2oxA1, VaGA2oxA2, VaGA2oxB1, VaGA2oxB2, and VaGA2oxB3, were cloned from etiolated adzuki bean (Vigna angularis cv. Dainagon) seedlings, and their enzymatic characteristics were examined using recombinant enzymes fused with glutathione S-transferase (GST). Recombinant VaGA2oxA1 (rVaGA2oxA1) and rVaGA2oxA2 showed 2beta-hydroxylation activity by converting GA1, GA4, GA9, GA20, GA4-methyl ester, and 16,17-dihydro-GA4 to the corresponding 2beta-hydroxylated gibberellins, which were identified by GC/MS. rVaGA2oxB1, rVaGA2oxB2, and rVaGA2oxB3 showed similar activity by converting [3H4]-16,17-dihydro-GA4 to a metabolite showing an Rf value of 16,17-dihydro-GA34. RNA-blot analysis showed that VaGA2oxA1 and VaGA2oxA2 were the major ones expressed in etiolated hypocotyls. The addition of Co2+ instead of Fe2+ to the assay medium apparently reduced the enzymatic activity, but increased the binding of [3H4]-16,17-dihydro-GA4 to rVaGA2oxA1, indicating the possibility that VaGA2oxs can be detected as gibberellin-binding proteins under certain conditions.

Amino Acid Sequence↗