【 摘 要 】
The orientation of a mitochondrial presequence peptide, associated with anionic lipid-containing model membranes, was investigated. The peptide inserts with its N-terminal α-helical part into cardiolipin (CL) monolayers so that the N-terminal 14 residues are protected from proteinase K. In phosphatidylglycerol (PG) monolayers the inserted peptide was fully accessible to the protease. A consequence of the different orientations of the peptide was that membrane potential-dependent protection from trypsin was much faster for the peptide bound to PG-containing vesicles compared to CL-containing membranes, suggesting that in the mitochondrial protein import process other components of the import apparatus are involved in the efficient potential-driven translocation of presequences across the inner mitochondrial membrane.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
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RO201912020302816ZK.pdf | 572KB | download |