Bacterial signal peptide recognizes HeLa cell mitochondrial import receptors and functions as a mitochondrial leader sequence |
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Authors: | A Mukhopadhyay L Ni C-S Yang H Weiner |
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Institution: | (1) Department of Biochemistry, Purdue University, 175 S. University Street, West Lafayette, Indiana 47907-2063, USA |
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Abstract: | Phage display was used to identify new components of the mammalian mitochondrial receptor complex using Tom20 as a binding partner. Two peptides were identified. One had partial identity (SMLTVMA) with a bacterial signal peptide from Toho-1, a periplasmic protein. The other had partial identity with a mitochondrial inner membrane glutamate carrier. The bacterial signal peptide could carry a protein into mitochondria both in vivo and in vitro. The first six residues of the sequence, SMLTVM, were necessary for import but the two adjacent arginine residues in the 30-amino-acid leader were not critical for import. The signal peptides of Escherichia coli β-lactamase and Bacillsus subtilis lipase could not carry proteins into mitochondria. Presumably, the Toho-1 leader can adopt a structure compatible for recognition by the import apparatus.Received 29 April 2005; received after revision 8 June 2005; accepted 17 June 2005 |
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Keywords: | Bacterial signal peptide mitochondrial protein import phage display Toho-1 twin-arginine Tom20 mitochondrial leader peptide |
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