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The Arabidopsis mutant dct is deficient in the plastidic glutamate/malate translocator DiT2
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| Zeitschriftentitel: | The Plant Journal |
|---|---|
| Personen und Körperschaften: | , , , , , , |
| In: | The Plant Journal, 35, 2003, 3, S. 316-331 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
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| Schlagwörter: |
| author_facet |
Renné, Petra Dreßen, Uta Hebbeker, Ulrike Hille, Diana Flügge, Ulf‐Ingo Westhoff, Peter Weber, Andreas P. M. Renné, Petra Dreßen, Uta Hebbeker, Ulrike Hille, Diana Flügge, Ulf‐Ingo Westhoff, Peter Weber, Andreas P. M. |
|---|---|
| author |
Renné, Petra Dreßen, Uta Hebbeker, Ulrike Hille, Diana Flügge, Ulf‐Ingo Westhoff, Peter Weber, Andreas P. M. |
| spellingShingle |
Renné, Petra Dreßen, Uta Hebbeker, Ulrike Hille, Diana Flügge, Ulf‐Ingo Westhoff, Peter Weber, Andreas P. M. The Plant Journal The Arabidopsis mutant dct is deficient in the plastidic glutamate/malate translocator DiT2 Cell Biology Plant Science Genetics |
| author_sort |
renné, petra |
| spelling |
Renné, Petra Dreßen, Uta Hebbeker, Ulrike Hille, Diana Flügge, Ulf‐Ingo Westhoff, Peter Weber, Andreas P. M. 0960-7412 1365-313X Wiley Cell Biology Plant Science Genetics http://dx.doi.org/10.1046/j.1365-313x.2003.01806.x <jats:title>Summary</jats:title><jats:p>The <jats:italic>Arabidopsis</jats:italic> mutant dicarboxylate transport (<jats:italic>dct</jats:italic>) is one of the classic mutants in the photorespiratory pathway. It requires high CO<jats:sub>2</jats:sub> levels for survival. Physiologic and biochemical characterization of <jats:italic>dct</jats:italic> indicated that <jats:italic>dct</jats:italic> is deficient in the transport of dicarboxylates across the chloroplast envelope membrane. Hence, re‐assimilation of ammonia generated by the photorespiratory cycle is blocked. However, the defective gene in <jats:italic>dct</jats:italic> has not been identified at the molecular level. Here, we report on the molecular characterization of the defective gene in <jats:italic>dct</jats:italic>, on the complementation of the mutant phenotype with a wild‐type cDNA, and on the functional characterization of the gene product, DiT2, in a recombinant reconstituted system. Furthermore, we provide the kinetic constants of recombinant DiT1 and DiT2, and we discuss these data with respect to their functions in ammonia assimilation. Moreover, an analysis of the transcript levels of DiT1 and DiT2 in different C<jats:sub>3</jats:sub>‐ and C<jats:sub>4</jats:sub>‐type plant species is presented, and we demonstrate that the substrate specificity of DiT2 from the C<jats:sub>4</jats:sub>‐plant <jats:italic>Flaveria bidentis</jats:italic> is similar to its counterpart from C<jats:sub>3</jats:sub> plants.</jats:p> The <i>Arabidopsis</i> mutant <i>dct</i> is deficient in the plastidic glutamate/malate translocator DiT2 The Plant Journal |
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| title |
The Arabidopsis mutant dct is deficient in the plastidic glutamate/malate translocator DiT2 |
| title_unstemmed |
The Arabidopsis mutant dct is deficient in the plastidic glutamate/malate translocator DiT2 |
| title_full |
The Arabidopsis mutant dct is deficient in the plastidic glutamate/malate translocator DiT2 |
| title_fullStr |
The Arabidopsis mutant dct is deficient in the plastidic glutamate/malate translocator DiT2 |
| title_full_unstemmed |
The Arabidopsis mutant dct is deficient in the plastidic glutamate/malate translocator DiT2 |
| title_short |
The Arabidopsis mutant dct is deficient in the plastidic glutamate/malate translocator DiT2 |
| title_sort |
the <i>arabidopsis</i> mutant <i>dct</i> is deficient in the plastidic glutamate/malate translocator dit2 |
| topic |
Cell Biology Plant Science Genetics |
| url |
http://dx.doi.org/10.1046/j.1365-313x.2003.01806.x |
| publishDate |
2003 |
| physical |
316-331 |
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<jats:title>Summary</jats:title><jats:p>The <jats:italic>Arabidopsis</jats:italic> mutant dicarboxylate transport (<jats:italic>dct</jats:italic>) is one of the classic mutants in the photorespiratory pathway. It requires high CO<jats:sub>2</jats:sub> levels for survival. Physiologic and biochemical characterization of <jats:italic>dct</jats:italic> indicated that <jats:italic>dct</jats:italic> is deficient in the transport of dicarboxylates across the chloroplast envelope membrane. Hence, re‐assimilation of ammonia generated by the photorespiratory cycle is blocked. However, the defective gene in <jats:italic>dct</jats:italic> has not been identified at the molecular level. Here, we report on the molecular characterization of the defective gene in <jats:italic>dct</jats:italic>, on the complementation of the mutant phenotype with a wild‐type cDNA, and on the functional characterization of the gene product, DiT2, in a recombinant reconstituted system. Furthermore, we provide the kinetic constants of recombinant DiT1 and DiT2, and we discuss these data with respect to their functions in ammonia assimilation. Moreover, an analysis of the transcript levels of DiT1 and DiT2 in different C<jats:sub>3</jats:sub>‐ and C<jats:sub>4</jats:sub>‐type plant species is presented, and we demonstrate that the substrate specificity of DiT2 from the C<jats:sub>4</jats:sub>‐plant <jats:italic>Flaveria bidentis</jats:italic> is similar to its counterpart from C<jats:sub>3</jats:sub> plants.</jats:p> |
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| author | Renné, Petra, Dreßen, Uta, Hebbeker, Ulrike, Hille, Diana, Flügge, Ulf‐Ingo, Westhoff, Peter, Weber, Andreas P. M. |
| author_facet | Renné, Petra, Dreßen, Uta, Hebbeker, Ulrike, Hille, Diana, Flügge, Ulf‐Ingo, Westhoff, Peter, Weber, Andreas P. M., Renné, Petra, Dreßen, Uta, Hebbeker, Ulrike, Hille, Diana, Flügge, Ulf‐Ingo, Westhoff, Peter, Weber, Andreas P. M. |
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| description | <jats:title>Summary</jats:title><jats:p>The <jats:italic>Arabidopsis</jats:italic> mutant dicarboxylate transport (<jats:italic>dct</jats:italic>) is one of the classic mutants in the photorespiratory pathway. It requires high CO<jats:sub>2</jats:sub> levels for survival. Physiologic and biochemical characterization of <jats:italic>dct</jats:italic> indicated that <jats:italic>dct</jats:italic> is deficient in the transport of dicarboxylates across the chloroplast envelope membrane. Hence, re‐assimilation of ammonia generated by the photorespiratory cycle is blocked. However, the defective gene in <jats:italic>dct</jats:italic> has not been identified at the molecular level. Here, we report on the molecular characterization of the defective gene in <jats:italic>dct</jats:italic>, on the complementation of the mutant phenotype with a wild‐type cDNA, and on the functional characterization of the gene product, DiT2, in a recombinant reconstituted system. Furthermore, we provide the kinetic constants of recombinant DiT1 and DiT2, and we discuss these data with respect to their functions in ammonia assimilation. Moreover, an analysis of the transcript levels of DiT1 and DiT2 in different C<jats:sub>3</jats:sub>‐ and C<jats:sub>4</jats:sub>‐type plant species is presented, and we demonstrate that the substrate specificity of DiT2 from the C<jats:sub>4</jats:sub>‐plant <jats:italic>Flaveria bidentis</jats:italic> is similar to its counterpart from C<jats:sub>3</jats:sub> plants.</jats:p> |
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| spelling | Renné, Petra Dreßen, Uta Hebbeker, Ulrike Hille, Diana Flügge, Ulf‐Ingo Westhoff, Peter Weber, Andreas P. M. 0960-7412 1365-313X Wiley Cell Biology Plant Science Genetics http://dx.doi.org/10.1046/j.1365-313x.2003.01806.x <jats:title>Summary</jats:title><jats:p>The <jats:italic>Arabidopsis</jats:italic> mutant dicarboxylate transport (<jats:italic>dct</jats:italic>) is one of the classic mutants in the photorespiratory pathway. It requires high CO<jats:sub>2</jats:sub> levels for survival. Physiologic and biochemical characterization of <jats:italic>dct</jats:italic> indicated that <jats:italic>dct</jats:italic> is deficient in the transport of dicarboxylates across the chloroplast envelope membrane. Hence, re‐assimilation of ammonia generated by the photorespiratory cycle is blocked. However, the defective gene in <jats:italic>dct</jats:italic> has not been identified at the molecular level. Here, we report on the molecular characterization of the defective gene in <jats:italic>dct</jats:italic>, on the complementation of the mutant phenotype with a wild‐type cDNA, and on the functional characterization of the gene product, DiT2, in a recombinant reconstituted system. Furthermore, we provide the kinetic constants of recombinant DiT1 and DiT2, and we discuss these data with respect to their functions in ammonia assimilation. Moreover, an analysis of the transcript levels of DiT1 and DiT2 in different C<jats:sub>3</jats:sub>‐ and C<jats:sub>4</jats:sub>‐type plant species is presented, and we demonstrate that the substrate specificity of DiT2 from the C<jats:sub>4</jats:sub>‐plant <jats:italic>Flaveria bidentis</jats:italic> is similar to its counterpart from C<jats:sub>3</jats:sub> plants.</jats:p> The <i>Arabidopsis</i> mutant <i>dct</i> is deficient in the plastidic glutamate/malate translocator DiT2 The Plant Journal |
| spellingShingle | Renné, Petra, Dreßen, Uta, Hebbeker, Ulrike, Hille, Diana, Flügge, Ulf‐Ingo, Westhoff, Peter, Weber, Andreas P. M., The Plant Journal, The Arabidopsis mutant dct is deficient in the plastidic glutamate/malate translocator DiT2, Cell Biology, Plant Science, Genetics |
| title | The Arabidopsis mutant dct is deficient in the plastidic glutamate/malate translocator DiT2 |
| title_full | The Arabidopsis mutant dct is deficient in the plastidic glutamate/malate translocator DiT2 |
| title_fullStr | The Arabidopsis mutant dct is deficient in the plastidic glutamate/malate translocator DiT2 |
| title_full_unstemmed | The Arabidopsis mutant dct is deficient in the plastidic glutamate/malate translocator DiT2 |
| title_short | The Arabidopsis mutant dct is deficient in the plastidic glutamate/malate translocator DiT2 |
| title_sort | the <i>arabidopsis</i> mutant <i>dct</i> is deficient in the plastidic glutamate/malate translocator dit2 |
| title_unstemmed | The Arabidopsis mutant dct is deficient in the plastidic glutamate/malate translocator DiT2 |
| topic | Cell Biology, Plant Science, Genetics |
| url | http://dx.doi.org/10.1046/j.1365-313x.2003.01806.x |