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.
Similar content being viewed by others
Author information
Authors and Affiliations
Corresponding author
Additional information
Received 29 April 2005; received after revision 8 June 2005; accepted 17 June 2005
Rights and permissions
About this article
Cite this article
Mukhopadhyay, A., Ni, L., Yang, CS. et al. Bacterial signal peptide recognizes HeLa cell mitochondrial import receptors and functions as a mitochondrial leader sequence. CMLS, Cell. Mol. Life Sci. 62, 1890–1899 (2005). https://doi.org/10.1007/s00018-005-5178-0
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00018-005-5178-0