Molecular cloning of a cDNA encoding aspartate aminotransferase-P2 from lupin root nodules

1992 ◽  
Vol 19 (3) ◽  
pp. 465-472 ◽  
Author(s):  
Paul H. S. Reynolds ◽  
Laura A. Smith ◽  
James M. J. J. Dickson ◽  
William T. Jones ◽  
Stephen D. Jones ◽  
...  
1999 ◽  
Vol 12 (4) ◽  
pp. 263-274 ◽  
Author(s):  
Hirofumi Yoshioka ◽  
Robert G. Gregerson ◽  
Deborah A. Samac ◽  
Kim C. M. Hoevens ◽  
Gian Trepp ◽  
...  

Aspartate aminotransferase (AAT) plays a critical role in the assimilation of symbiotically fixed nitrogen into aspartate and asparagine in legume root nodules. The enzyme occurs as a cytosolic form (AAT1) and a plastid form (AAT2) in alfalfa nodules. To elucidate the functional role of each isozyme in root nodule metabolism further, in situ hybridization was used to determine the pattern of transcript accumulation from the two genes. AAT2 transcripts were localized to infected cells throughout the symbiotic zone of effective alfalfa nodules; however, expression was reduced in ineffective nodules. The AAT1 gene was expressed in the uninfected cells of the invasion zone and symbiotic zone, the nodule parenchyma, and nodule vascular bundles of both effective and ineffective nodules. The AAT1 and AAT2 promoters were evaluated in transgenic alfalfa plants containing promoter β-glucuronidase (GUS) gene fusions. Histochemical staining patterns agreed with results from in situ localization. The distribution pattern of gene transcripts suggests that AAT1 has a role in maintenance of the O2 diffusion barrier in nodules and that AAT2 plays a major role in assimilation of recently fixed nitrogen. Promoter deletion analysis of the AAT2 promoter revealed that nodule-specific expression was retained in a promoter fragment of 300 bp.


1990 ◽  
Vol 94 (4) ◽  
pp. 1634-1640 ◽  
Author(s):  
Mark W. Farnham ◽  
Stephen M. Griffith ◽  
Susan S. Miller ◽  
Carroll P. Vance

1992 ◽  
Vol 19 (2) ◽  
pp. 147 ◽  
Author(s):  
WT Jones ◽  
SD Jones ◽  
CP Liddane ◽  
PHS Reynolds

Leguminous root nodules contain two forms of aspartate aminotransferase (AAT). AAT-P1 is con- stitutively expressed in roots and nodules, whereas the second isoenzyme, AAT-P2, is induced in developing nodules. A two site ELISA system was developed to quantify AAT-P2 in nodule extracts. The assay comprised two affinity-purified monoclonal antibodies directed against different epitopes on the AAT-P2 molecule. The sensitivity was less than 200 pg mL-1, and AAT-P2 could be quantified in the range 1 to 15 ng mL-1. The assay was specific for AAT-P2, and did not measure AAT-P1. The assay was used to specifically measure AAT-P2 in the developing legume root nodule formed by the symbiotic liaison between Rhizobium lupini NZP2257 and the roots of Lupinus angustifolius L. The ELISA method, which measures AAT-P2 protein, was contrasted with an approach which relied on the heat lability of AAT-P2 at 60°C to measure individual isoenzyme catalytic activity.


1989 ◽  
Vol 90 (4) ◽  
pp. 1622-1629 ◽  
Author(s):  
Stephen M. Griffith ◽  
Carroll P. Vance

1990 ◽  
Vol 94 (3) ◽  
pp. 1358-1364 ◽  
Author(s):  
William T. Jones ◽  
Paul H. S. Reynolds ◽  
Stephen D. Jones ◽  
Cherry P. Liddane ◽  
Karen A. Rodber

1988 ◽  
Vol 103 (5) ◽  
pp. 797-804 ◽  
Author(s):  
Yoshiyuki Horio ◽  
Tatsuya Tanaka ◽  
Masato Taketoshi ◽  
Fujio Nagashima ◽  
Sumio Tanase ◽  
...  

1987 ◽  
Vol 149 (3) ◽  
pp. 859-865 ◽  
Author(s):  
Joseph R. Mattingly ◽  
Francisco J. Rodriguez-Berrocal ◽  
Jack Gordon ◽  
Ana Iriarte ◽  
Marino Martinez-Carrion

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