T-protein of the glycine decarboxylase multienzyme complex: evidence for partial similarity to formyltetrahydrofolate synthetase |
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| Authors: | Stanislav Kopriva Simon R. Turner Stephen Rawsthorne Hermann Bauwe |
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| Affiliation: | (1) Department of Molecular Cell Biology, Institute of Plant Genetics and Crop Plant Research, Corrensstrasse 3, 06466 Gatersleben, Germany;(2) Department of Brassica and Oilseeds Research, John Innes Centre, Colney, NR4 7UH Norwich, UK;(3) Present address: Carnegie Institute of Plant Biology, 290 Panama Street, 94304 Stanford, CA, USA |
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| Abstract: | We have isolated and sequenced cDNA clones encoding T-protein of the glycine decarboxylase complex from three plant species, Flaveria pringlei, Solanum tuberosum and Pisum sativum. The predicted amino acid sequences of these clones are at least 87% identical and all are similar to the predicted sequences of the bovine, human, chicken and Escherichia coli T-proteins. Alignment of all these sequences revealed conserved domains, one of which showed a significant similarity to a part of the formyltetrahydrofolate synthetases from procaryotes and eucaryotes. This suggests that the T-protein sequence is not as unique as previously thought. |
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| Keywords: | glycine cleavage system T-protein THF binding site |
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