Identification of hydrophobic residues in the signal sequence of mitochondrial preornithine carbamyltransferase that enhance the rate of precursor import.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference31 articles.
1. Effects of Synthetic Model Peptides Resembling the Extension Peptides of Mitochondrial Enzyme Precursors on Import of the Precursors into Mitochondria1
2. A synthetic signal peptide blocks import of precursor proteins destined for the mitochondrial inner membrane or matrix.
3. A chemically synthesized pre-sequence of an imported mitochondrial protein can form an amphiphilic helix and perturb natural and artificial phospholipid bilayers.
4. Structural analysis and amphiphilic properties of a chemically synthesized mitochondrial signal peptide.
5. Incorporation of a synthetic mitochondrial signal peptide into charged and uncharged phospholipid monolayers
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1. The loss in hydrophobic surface area resulting from a Leu to Val mutation at the N-terminus of the aldehyde dehydrogenase presequence prevents import of the protein into mitochondria;Protein Science;2008-12-31
2. Positively charged residues, the helical conformation and the structural flexibility of the leader sequence of pALDH are important for recognition by hTom20;FEBS Letters;1999-11-08
3. In Vivo Mitochondrial Import;Journal of Biological Chemistry;1999-04
4. An Amphiphilic Lipid-Binding Domain Influences the Topology of a Signal-Anchor Sequence in the Mitochondrial Outer Membrane;Biochemistry;1996-01-01
5. Insertion of an uncharged polypeptide into the mitochondrial inner membrane does not require a trans-bilayer electrochemical potential: effects of positive charges;Biochimica et Biophysica Acta (BBA) - Biomembranes;1995-07
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