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Seasonal variation of leaf glutamine synthetase isoforms in temperate deciduous trees strongly suggests different functions for the enzymes
Author(s) -
PEARSON J.,
JI Y.M.
Publication year - 1994
Publication title -
plant, cell and environment
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.646
H-Index - 200
eISSN - 1365-3040
pISSN - 0140-7791
DOI - 10.1111/j.1365-3040.1994.tb00535.x
Subject(s) - glutamine synthetase , nitrate reductase , biology , nitrogen assimilation , temperate deciduous forest , deciduous , botany , enzyme assay , isozyme , enzyme , glutamine , biochemistry , amino acid
Changes in the activities of leaf glutamine synthetase (GS) isoforms were followed in four temperate deciduous trees from full leaf expansion to senescence (May to November). In the early part of the season, total GS activity was high in all species, with values ranging from 90 to 200 μmol h −1 g −1 fw. During this early period this activity comprised only the activity of the chloroplastic (GS 2 ) isoform in all species. These high GS 2 activities are consistent with the role of GS 2 in the re‐assimilation of photorespired ammonia. The early high values also coincided with high nitrate reductase activity in one of the species, the highly nitrophilous species Sambucus nigra , with values of up to 16μmol h −1 g −1 fw. This indicates that GS 2 is also important in the assimilation of ammonia produced from nitrate reduction. From mid‐ to late‐season, the cytosolic isoform (GS 1 ) was detected in all four species and became increasingly more active in comparison to GS 2 . By the time of senescence it was the dominant enzyme of the two forms in both S. nigra and Carpinus betulus. The results provide strong support for recent findings that GS 1 is an important enzyme for the mobilization of nitrogen for translocation or storage.