A modifiedEscherichia coli chaperonin (groEL) polypeptide synthesized in tobacco and targeted to the chloroplasts |
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Authors: | Huacheng B Wu Gina L Feist Sean M Hemmingsen |
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Institution: | (1) Plant Biotechnology Institute, National Research Council Canada, 110 Gymnasium Place, S7N 0W9 Saskatoon, Saskatchewan, Canada |
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Abstract: | The coding region for theEscherichia coli groEL (chaperonin-60) polypeptide was fused downstream of a pea rubisco small subunit transit peptide coding sequence under the control of a tandem 35S CaMV promoter. Transgenic tobacco plants (Nicotiana tabacum cv. Xanthi) containing this modifiedgroEL gene were produced. The modified groEL polypeptide was correctly imported into chloroplasts and accumulated to high or low levels in different plants. The majority of the modified groEL polypeptide was processed correctly to the mature form within the chloroplasts. Approximately 20% of the imported polypeptides retained a portion of the N-terminal transit peptide (TPgroEL). Both groEL and TPgroEL polypeptides assembled into tetradecameric species in the chloroplasts. In plants accumulating high levels of these products, the majority of the plant chaperonin-60 polypeptides in the chloroplast were present in novel hybrid tetradecameric species containing both bacterial and plant chaperonin-60 polypeptides. In plants accumulating low levels of groEL, the predominant species present appeared to be authentic plant cpn6014 and authentic bacterial groEL14. The growth and development of transgenic and control tobacco plants were indistinguishable.Abbreviations cpn60
chaperonin-60
- cpn10
chaperonin-10
- hsp
heat shock protein
- rubisco
ribulose-1,5-bisphosphate carboxylase-oxygenase
- ssu
small subunit
- spp
stromal processing peptidase
- SDS
sodium dodecyl sulfate
- PAGE
polyacrylamide gel electrophoresis |
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Keywords: | chaperonin assembly chaperonin hybrids chloroplast targeting |
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