Normal growth of transgenic tobacco plants in the absence of cytosolic pyruvate kinase

The coding sequence of the cytosolic isozyme of Potato tuber pyruvate kinase (PK) was attached to the transit peptide of the small subunit of pea ribulose-1,5-bisphosphate carboxylase oxygenase and placed under the control of the cauliflower mosaic virus 35S promoter. This construct was transformed...

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Bibliographic Details
Published in:Plant physiology (Bethesda) 1992-10, Vol.100 (2), p.820-825
Main Authors: Gottlob-McHugh, S.G, Sangwan, R.S, Blakeley, S.D, Vanlerberghe, G.C, Ko, K, Turpin, D.H, Plaxton, W.C, Miki, B.L, Dennis, D.T
Format: Article
Language:English
Subjects:
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
ADN RECOMBINADO
ADN RECOMBINE
Agronomy. Soil science and plant productions
Biological and medical sciences
Biotechnology
CITOPLASMA
Complementary DNA
CRECIMIENTO
CROISSANCE
CYTOPLASME
DNA
DNA probes
ECHANGE GAZEUX
ENFERMEDADES CARENCIALES
ENZIMAS
ENZYME
Enzymes
FEUILLE
FOTOSINTESIS
Fundamental and applied biological sciences. Psychology
GENE
GENES
HOJAS
Immunology
INTERCAMBIO DE GASES
Leaves
MALADIE DE CARENCE
Metabolism
Metabolism and Enzymology
NICOTIANA TABACUM
PEPTIDE
PEPTIDOS
PHOTOSYNTHESE
Photosynthesis, respiration. Anabolism, catabolism
PIRUVATO QUINASA
Plant physiology and development
Plants
Plastids
PYRUVATE KINASE
RIBULOSA-BIFOSFATO CARBOXILASA
RIBULOSE-BISPHOSPHATE CARBOXYLASE
RNA
SOLANUM TUBEROSUM
TRANSFORMACION GENETICA
TRANSFORMATION GENETIQUE
Transgenic plants
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Summary:The coding sequence of the cytosolic isozyme of Potato tuber pyruvate kinase (PK) was attached to the transit peptide of the small subunit of pea ribulose-1,5-bisphosphate carboxylase oxygenase and placed under the control of the cauliflower mosaic virus 35S promoter. This construct was transformed into Nicotiana tabacum. Unexpectedly, two primary transformants were recovered in which PK activity in leaves was greatly reduced. The reduction in PK activity appeared to result from the complete absence of the cytosolic form of the enzyme(PKc). In addition, no PKc could be detected on western blots of leaf extracts. Metabolite analyses indicated that the levels of phosphoenolpyruvate are substantially higher in PKc-deficient leaves than in wild-type leaves, consistent with a block in glycolysis at the step catalyzed by PK. PKc deficiency in the leaves does not appear to adversely affect plant growth. Analysis of progeny indicates that PKc deficiency is a heritable trait. The leaves of PKc-deficient transformants have normal rates of photosynthetic evolution and respiratory consumption, indicating that these plants are using alternative pathways to bypass PK
ISSN:0032-0889
1532-2548
DOI:10.1104/pp.100.2.820