Truncated presequences of mitochondrial F1-ATPase β subunit from Nicotiana plumbaginifolia transport CAT and GUS proteins into mitochondria of transgenic tobacco
| Autor: | François Chaumont, S. Leterme, Marc Boutry, Didier Thomas, M de Castro Silva Filho |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Chloramphenicol O-Acetyltransferase
Recombinant Fusion Proteins ATPase Molecular Sequence Data Plant Science Protein Sorting Signals medicine.disease_cause chemistry.chemical_compound Genes Reporter Tobacco Protein targeting Genetics medicine Amino Acid Sequence Protein Precursors Nicotiana plumbaginifolia Gene Glucuronidase Sequence Deletion Reporter gene Methionine biology fungi Nucleic acid sequence food and beverages Biological Transport General Medicine Plants Genetically Modified Fusion protein Mitochondria Plants Toxic Proton-Translocating ATPases Biochemistry chemistry biology.protein Protein Processing Post-Translational Sequence Analysis Agronomy and Crop Science |
| Zdroj: | Plant Molecular Biology. 24:631-641 |
| ISSN: | 1573-5028 0167-4412 |
| Popis: | The mitochondrial F1-ATPase beta subunit (ATPase-beta) of Nicotiana plumbaginifolia is nucleus-encoded as a precursor containing an NH2-terminal extension. By sequencing the mature N. tabacum ATPase-beta, we determined the length of the presequence, viz. 54 residues. To define the essential regions of this presequence, we produced a series of 3' deletions in the sequence coding for the 90 NH2-terminal residues of ATPase-beta. The truncated sequences were fused with the chloramphenicol acetyl transferase (cat) and beta-glucuronidase (gus) genes and introduced into tobacco plants. From the observed distribution of CAT and GUS activity in the plant cells, we conclude that the first 23 amino-acid residues of ATPase-beta remain capable of specifically targeting reporter proteins into mitochondria. Immunodetection in transgenic plants and in vitro import experiments with various CAT fusion proteins show that the precursors are processed at the expected cleavage site but also at a cryptic site located in the linker region between the presequence and the first methionine of native CAT. |
| Databáze: | OpenAIRE |
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