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

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.

2010 ◽  
Vol 154 (4) ◽  
pp. 1842-1854 ◽  
Author(s):  
Taiji Kawakatsu ◽  
Sakiko Hirose ◽  
Hiroshi Yasuda ◽  
Fumio Takaiwa

2005 ◽  
Vol 32 (11) ◽  
pp. 997 ◽  
Author(s):  
Elke G. Rosche ◽  
Daniel Blackmore ◽  
Christina E. Offler ◽  
John W. Patrick

Pea (Pisum sativum L.) cotyledons, overexpressing a potato sucrose transporter (StSUT1), were used to explore the hypothesis that sucrose stimulates the onset of storage protein biosynthesis. The study focused on the transition between pre-storage and storage phases of seed development. During this period supply of sucrose and hexose to transgenic cotyledons was unaffected by StSUT1 expression. However, protoplasmic levels of sucrose but not hexoses were elevated in transgenic cotyledons. Total protein levels in cotyledons followed the same temporal trend as observed for sucrose and this was reflected in an earlier appearance of protein bodies. Protein levels in wild type and StSUT1 cotyledons were found to lie on the same sucrose dose-response curve and this could be reproduced in vitro when wild type cotyledons were cultured on media containing various sucrose concentrations. Rates of [14C]sucrose uptake and incorporation into polymeric forms were consistent with protoplasmic sucrose supplying a proportion of the carbon skeletons required for storage protein accumulation. In addition, vicilin gene expression was up-regulated earlier in StSUT1 cotyledons. We conclude that sucrose functions both as a signal and fuel to stimulate storage protein accumulation and assembly into protein bodies. An earlier stimulation of storage protein synthesis is considered to largely account for the 14% increase in protein levels of StSUT1 seeds at harvest.


1993 ◽  
Vol 374 (7-12) ◽  
pp. 887-894 ◽  
Author(s):  
Mathias WENZEL ◽  
Heinrich GERS-BARLAG ◽  
Anneliese SCHIMPL ◽  
Harold RÜDIGER

2009 ◽  
Vol 29 (1) ◽  
pp. 87-95 ◽  
Author(s):  
Yoichi Kita ◽  
Yumi Nakamoto ◽  
Masakazu Takahashi ◽  
Keisuke Kitamura ◽  
Kyo Wakasa ◽  
...  

1968 ◽  
Vol 21 (4) ◽  
pp. 827 ◽  
Author(s):  
MJ Hynes

A number of electrophoretic variants of plant enzymes have been described and the genetic control of these variants determined (e.g. Beckman, Scandalios, and Brewbaker 1964; Schwartz 1964; Scandalios 1965). However, little work has been done on structural and storage proteins of plants. Varietal differences have been observed in the electrophoretic patterns of wheat storage proteins (Graham and Morton 1963) and two forms of arachin, a storage protein of the peanut, have been described (Tombs 1964), though no genetic studies of these differences have been made. This communication describes the detection and the partial characterization of variants of proteins extracted from the cotyledons of Pisum sativum seeds and some preliminary breeding tests to determine their genetic control.


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