Import inhibition of poly(His) containing chloroplast precursor proteins by Ni2+ ions
| Autor: | Arminio Boschetti, M Thiess, P Schumann, R Rothen |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
inorganic chemicals
Chloroplasts medicine.medical_treatment Recombinant Fusion Proteins Ribulose-Bisphosphate Carboxylase Biophysics Chlamydomonas reinhardtii Ni2+ inhibition Biochemistry Nickel Structural Biology medicine Genetics Animals Histidine Cloning Molecular Protein Precursors Molecular Biology Chloroplast protein import Protease Chlamydomonas reinhardii biology Dose-Response Relationship Drug Chlamydomonas RuBisCO Inhibition by nickel ions Biological Transport Cell Biology biology.organism_classification Hsp70 Pyruvate carboxylase Chloroplast stomatognathic diseases biology.protein |
| Zdroj: | FEBS Letters. 403:15-18 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/s0014-5793(97)00016-1 |
| Popis: | The precursor of the small subunit of ribulose-1,5-bisphosphate carboxylase (pSS) and a modified pSS containing a C-terminal hexahistidyl tail (pSS(His)6) were imported into isolated Chlamydomonas chloroplasts with comparable efficiency. In the presence of Ni2+ ions the import of pSS(His)6 was inhibited and the precursor bound to the envelope remained protease sensitive, while import of pSS was not affected. Addition of an excess of l-histidine suppressed the inhibition demonstrating that the hexahistidyl-Ni2+ complex was responsible for import inhibition. Inhibition could be observed between about 0.5 and 10 mM Ni2+, depending on the total protein content in the assay. Import incompetent Ni2+-precursor complexes can be used to study early events in chloroplast protein import.© 1997 Federation of European Biochemical Societies. |
| Databáze: | OpenAIRE |
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