Conformational changes of a mitochondrial precursor protein on binding to phospholipid vesicles and SDS micelles A circular dichroism and fluorescence spectroscopy study
- 5 June 1989
- journal article
- Published by Wiley in FEBS Letters
- Vol. 249 (2) , 173-177
- https://doi.org/10.1016/0014-5793(89)80618-0
Abstract
Conformations of an artificial mitochondrial precursor protein pCox IV‐DHFR have been analyzed by CD and fluorescence spectroscopy in the presence of (cardiolipin‐rich) phospholipid vesicles or SDS micelles. Binding of pCox IV‐DHFR to phospholipid vesicles involves a conformational change, which is presequence‐dependent, accompanies alteration in the secondary structure of the DHFR moiety, but is different from total unfolding of the polypeptide chain. On the other hand, a conformational change of the fusion protein on binding to the micelles of a positively charged detergent, SDS, is not presequence‐dependent.Keywords
This publication has 14 references indexed in Scilit:
- A chimeric mitochondrial precursor protein with internal disulfide bridges blocks import of authentic precursors into mitochondria and allows quantitation of import sites.The Journal of cell biology, 1988
- Import of proteins into mitochondria: a multi‐step processEuropean Journal of Biochemistry, 1988
- Protein unfolding and the energetics of protein translocation across biological membranesCell, 1988
- Binding of a specific ligand inhibits import of a purified precursor protein into mitochondriaNature, 1986
- Apocytochrome c Induces pH-Dependent Vesicle FusionMembrane Biochemistry, 1986
- Investigations on the insertion of the mitochondrial precursor protein apocytochrome c into model membranesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1985