scholarly journals Photoperiod Control of Poplar Bark Storage Protein Accumulation

1991 ◽  
Vol 96 (3) ◽  
pp. 686-692 ◽  
Author(s):  
Gary D. Coleman ◽  
Tony H. H. Chen ◽  
Stephen G. Ernst ◽  
Leslie Fuchigami
Keyword(s):  
Storage Protein ◽  
Protein Accumulation ◽  
Bark Storage Protein ◽  
Photoperiod Control

Transcriptional and metabolic alternations rebalance wheat grain storage protein accumulation under variable nitrogen and sulfur supply

2015 ◽  
Vol 83 (2) ◽  
pp. 326-343 ◽  
Author(s):  
Zhanwu Dai ◽  
Anne Plessis ◽  
Jonathan Vincent ◽  
Nathalie Duchateau ◽  
Alicia Besson ◽  
...  
Keyword(s):  
Storage Protein ◽  
Grain Storage ◽  
Protein Accumulation ◽  
Wheat Grain ◽  
Sulfur Supply

scholarly journals Sequence of a Poplar Bark Storage Protein Gene

1993 ◽  
Vol 102 (4) ◽  
pp. 1347-1348 ◽  
Author(s):  
G. D. Coleman ◽  
THH. Chen
Keyword(s):  
Storage Protein ◽  
Protein Gene ◽  
Storage Protein Gene ◽  
Bark Storage Protein

Amino acid transporter expression and localisation studies in pea (Pisum sativum)

2007 ◽  
Vol 34 (11) ◽  
pp. 1019 ◽  
Author(s):  
Mechthild Tegeder ◽  
Qiumin Tan ◽  
Aleel K. Grennan ◽  
John W. Patrick
Keyword(s):  
Amino Acid ◽  
Pisum Sativum ◽  
Storage Protein ◽  
Expression Patterns ◽  
Phloem Loading ◽  
Transfer Cells ◽  
Protein Accumulation ◽  
Developmentally Regulated ◽  
And Storage ◽  
Seed Coats

Expression of the amino acid permeases PsAAP1 and PsAAP2 was analysed in developing pea (Pisum sativum L.) plants. Both transporters were expressed in seed coats and cotyledon epidermal transfer cells and storage parenchyma cells. AAP expression is developmentally regulated and coincides with the onset of storage protein synthesis. Nitrogen was shown to induce AAP expression and AAP transcript levels were upregulated during the photoperiod. Analysis of Arabidopsis thaliana AAP1 promoter activity in pea, using promoter-β-glucuronidase (promotor-GUS) studies, revealed targeting of GUS to seed coats and cotyledon epidermal transfer cells. Expression was found in the nutritious endosperm during the early stages of seed development, whereas GUS staining in embryos was detected from the heart stage onward. In addition, AAP1 expression was observed in the phloem throughout the plant. This finding equally applied to PsAAP1 expression as shown by in situ mRNA hybridisation, which also demonstrated that PsAAP1 expression was localised to companion cells. Overall, PsAAP1 expression patterns and cellular localisation point to a function of the transporter in phloem loading of amino acids for translocation to sinks and in seed loading for development and storage protein accumulation.

Control of storage protein accumulation during legume seed development

2001 ◽  
Vol 158 (4) ◽  
pp. 457-464 ◽  
Author(s):  
Sabine Golombek ◽  
Hardy Rolletschek ◽  
Ulrich Wobus ◽  
Hans Weber
Keyword(s):  
Seed Development ◽  
Storage Protein ◽  
Protein Accumulation ◽  
Legume Seed

scholarly journals Identification and expression analysis of a novel phytocystatin in developing and germinating seeds of triticale (×Triticosecale Wittm.)

2015 ◽  
Vol 84 (1) ◽  
pp. 139-142 ◽  
Author(s):  
Joanna Simińska ◽  
Wiesław Bielawski
Keyword(s):  
Seed Germination ◽  
Seed Development ◽  
Storage Protein ◽  
Cdna Sequence ◽  
Storage Proteins ◽  
Cysteine Proteinase ◽  
Protein Accumulation ◽  
Protein Levels ◽  
Germinating Seeds ◽  
Cysteine Proteinase Activity

In this paper the complete cDNA sequence of a newly identified triticale phytocystatin, TrcC-7, was analyzed. Because <em>TrcC-7</em> transcripts were present in seeds, we hypothesized that it may regulate storage protein accumulation and degradation. Therefore, changes in mRNA and protein levels during the entire period of seed development and germination were examined. Expression of <em>TrcC-7</em> increased during development and decreased at the end of maturation and subsequently increased during seed germination. Based on these results, TrcC-7 likely regulates cysteine proteinase activity during the accumulation and mobilization of storage proteins.

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