Hexose-transport-deficient mutants of Chlorella vulgaris |
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Authors: | N Sauer |
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Institution: | (1) Institut für Botanik, Universität Regensburg, Universitätsstrasse 31, D-8400 Regensburg, Germany;(2) Present address: Plant Biology Laboratory, Salk Institute, P.O. Box 85800, 92138 San Diego, CA, USA |
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Abstract: | Autotrophically grown cells of Chlorella vulgaris show a strong increase in the uptake rates for hexoses and for seven amino acids when incubated in the presence of hexoses. This increase is due to de-novo synthesis of three transport proteins: one forhexoses and two for amino acids. Mutants deficient in hexose transport were obtained after treatment of wild-type cells with acridine orange, followed by a selection procedure using the toxic hexose analogue, 2-deoxy-D-glucose. Moreover, the two amino-acid-transport systems could not be induced in these mutants by hexoses. The capacity to phosphorylate hexoses was identical in mutants and in the wild-type strain. The loss of transport activities can be correlated with the loss of certain radiolabeled protein bands on fluorograms of sodium dodecylsulfate-polyacrylamide gels. These proteins are assumed to be responsible for the different transport systems in the wild-type strain. With the help of additional mutants defective in one or two of the different aminoacid-transport systems, it has been attempted to assign the different transport activities to individual protein bands on the gel.Abbreviations AUP
arginine-uptake-defective mutant
- 2-DG
2-deoxy-D-glucose
- 6-DG
6-deoxy-D-glucose
- HUP
hexose-uptake-defective mutant
- PUP-
proline-uptake-defective mutant
- SDS
sodium dodecyl sulfate
- WT
wild type |
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Keywords: | Amino acid transport Chlorella Hexose transport Mutant (Chlorella) Transport (protein) |
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