Photoperiod Control of Poplar Bark Storage Protein Accumulation

Coleman, Gary D.; Chen, Tony H. H.; Ernst, Stephen G.; Fuchigami, Leslie H.

doi:10.1104/pp.96.3.686

Cited by 117 publications

(101 citation statements)

References 29 publications

(23 reference statements)

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“…7). This protein band corresponds in size to VSP previously characterized in poplar bark (Coleman et al, 1991;Langheinrich & Tischner, 1991). The comparison between stained SDS-PAGE gels from control and transgenic plants showed that the 32-kDa polypeptide accumulated in transgenic stems more quickly than in control plants (Fig.…”

Section: Tree Growth and Gs1 Content In Leafmentioning

confidence: 99%

Improved growth in a field trial of transgenic hybrid poplar overexpressing glutamine synthetase

et al. 2004

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Summary• In the present work the performance of transgenic poplars expressing a pine glutamine synthetase (GS) transgene was studied in natural conditions.• A field study of eight independent transgenic lines and control plants was carried out for 3 yr in the province of Granada (Spain).• Transgenic poplars reached average heights that were 21, 36 and 41% greater than control plants after the first, second and third year of growth, respectively. Transgene expression affected plant features with time resulting in increased protein, total GS and ferredoxin-dependent glutamate synthase (Fd-GOGAT) in leaves. However, neither differences in the large subunit of Rubisco (LSU) abundance nor water content were detected between lines. Furthermore, no significant differences were found in total polysaccharide and lignin content in tree trunks.• The analyses of stem diameter, and protein contents in the bark suggest that higher levels of nitrogen reserves accumulated in the stem of transgenics. Our results suggest that modification of GS1 expression may be a useful strategy to complement traditional tree breeding in short rotation plantations.

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Section: Tree Growth and Gs1 Content In Leafmentioning

confidence: 99%

Improved growth in a field trial of transgenic hybrid poplar overexpressing glutamine synthetase

et al. 2004

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“…Hybridizations were carried out in the same buffer overnight at 65°C. RNA blots were washed once in lx SSC and 0.1% SDS at room temperature for 20 (1). The library was screened with BSP antiserum resulting in one positive clone/ 1300 plaqueforming units.…”

Section: Protein Sequencingmentioning

confidence: 99%

“…Poplar BSP was partially purified as described previously (1). Approximately 1000 pmol of partially purified protein was further purified by SDS-PAGE and blotted to polyvinylidene difluoride membrane (Immobilon P, Millipore) as described by LeGendre and Matsudaira (12).…”

Section: Protein Sequencingmentioning

confidence: 99%

“…During spring shoot growth, the storage vacuoles are replaced by a large central vacuole, and BSPs disappear or are reduced to low levels. In poplar, the accumulation of a 32-kD BSP is controlled by photoperiod, with SDs stimulating accumulation and LDs inhibiting accumulation (1). The accumulation of poplar BSP is also correlated with changes in the population of translatable mRNA (1).…”

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confidence: 99%

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Complementary DNA Cloning of Poplar Bark Storage Protein and Control of Its Expression by Photoperiod

Coleman¹,

Chen²,

Fuchigami³

1992

Plant Physiol.

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Bark storage proteins accumulate in the bark of many woody plants during autumn and winter. In poplar (Populus de/toides Bartr. ex Marsh), the accumulation of the 32-kilodalton bark storage protein is controlled by photoperiod. We have isolated a full-length cDNA encoding for the poplar 32-kilodalton bark storage protein and determined its nucleotide sequence. The derived amino acid sequence shows that poplar bark storage protein is rich in serine, leucine, phenylalanine, and lysine. Poplar bark storage protein is similar to the poplar wound-induced cDNA clone 4 and clone 16 (TJ Parsons, HD Bradshaw, MP Gordon [1989] Proc NatI Acad Sci USA 86: 7895-7899). DNA gel blot analysis suggests that poplar bark storage protein is encoded by a multigene family of about five genes. Poplar plants grown in long days contained low levels of mRNA for the bark storage protein. Exposure to short days resulted in an increase in bark storage protein mRNA within 7 days. After 21 days of short day exposure, high levels of mRNA were detected. The accumulation of bark storage protein mRNA in response to short days was also observed in plants exposed to natural shortening daylengths. Our results indicate that the accumulation of poplar bark storage protein mRNA is controlled by photoperiod. This finding will provide a useful system for investigating photoperiodism in woody plants.

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“…In addition, a variety of storage proteins have been detected in bark and other tissues of hardwoods and softwoods (Coleman et al, 1991;Wetzel et al, 1991;Harms and Sauter, 1992). These studies point to the diverse locations of VSP throughout the plant body and also illustrate the physiological and biochemical mechanisms that different tissues use to store nutrients.…”

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confidence: 99%

Expression of Sporophytic Storage Proteins in the Corm of the Quillwort (Isoetes echinospora Dur.)

1994

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Parenchyma cells from the corm tissue of the aquatic lycopod lsoefes echinospora Dur. were shown by electron microscopy to be packed with amyloplasts, lipid bodies, and protein bodies. The protein bodies are morphologically similar to those identified in seeds and certain vegetative tissues of higher plants. Globoidcontaining protein bodies (1-10 pm) isolated in a sucrose gradient possessed a buoyant density of 1.28 g/mL and contained globulin (salt-soluble) proteins. Sucrose gradient centrifugation of crude globulins revealed only two components with mean sedimentation coefficients of approximately 2s and 11s. The 2s component, designated VSP-lsA, was composed of a 15.7-kD polypeptide. The 11s component, designated VSP-lsB, had a molecular mass of 215 kD as estimated by gel filtration and was composed of 39-to 42-kD polypeptides. Two-dimensional gel electrophoresis showed constituent polypeptides distinguished by differences in net charge and molecular mass. Affinity-purified antibodies against VSP-lsA and VSP-lsB prepared and used as probes on immunoblots crossreact only with their specific antigens, suggesting that the proteins are not immunologically related. Indirect immunolocalization studies confirmed that VSP-lsB is deposited in protein bodies. These globulin proteins, like those from some seeds, form the principal storage reserves of the corm tissue.

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Photoperiod Control of Poplar Bark Storage Protein Accumulation

Cited by 117 publications

References 29 publications

Improved growth in a field trial of transgenic hybrid poplar overexpressing glutamine synthetase

Improved growth in a field trial of transgenic hybrid poplar overexpressing glutamine synthetase

Complementary DNA Cloning of Poplar Bark Storage Protein and Control of Its Expression by Photoperiod

Expression of Sporophytic Storage Proteins in the Corm of the Quillwort (Isoetes echinospora Dur.)

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