Document Detail

Factors involved in the coordinate appearance of nitrite reductase and glutamine synthetase in the mustard (Sinapis alba L.) seedling.
MedLine Citation:
PMID:  24202024     Owner:  NLM     Status:  In-Data-Review    
The extent to which the appearances of nitrite reductase (NIR; EC and glutamine synthetase (GS; EC are coordinated was studied in mustard (Sinapis alba L.) seedlings. It was established by immunotitration that the increased activities of NIR and GS in the presence of light and nitrate can be attributed to the de-novo synthesis of enzyme protein. The bulk of the NIR and GS was found in the developing cotyledons. In the absence of nitrate in the growth medium there was no coordinate appearance of NIR and GS. While light strongly stimulated the appearance of GS, the level of NIR was hardly affected and remained low. On the other hand, in the presence of nitrate in the medium the appearances of NIR and GS were strictly coordinated, the GS level being considerably above that of NIR. It is argued that phytochrome-controlled synthesis of GS in the absence of nitrate is part of the mechanism to reassimilate ammonium liberated during proteolysis of storage protein and metabolism of the resulting amino acids, whereas the strictly coordinated synthesis in the presence of light and nitrate indicates the dominance of nitrate assimilation under these circumstances. The fact that the level of GS was always considerably above that of NIR appears to be a safety measure to prevent ammonium accumulation.
M Weber; S Schmidt; C Schuster; H Mohr
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Planta     Volume:  180     ISSN:  0032-0935     ISO Abbreviation:  Planta     Publication Date:  1990 Feb 
Date Detail:
Created Date:  2013-11-08     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  1250576     Medline TA:  Planta     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  429-34     Citation Subset:  -    
Biologisches Institut II der Universität, Schänzlestrasse 1, D-7800, Freiburg i.Br., Germany.
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