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pubmed-article:16041565pubmed:abstractTextPhage 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 beta-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.lld:pubmed
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pubmed-article:16041565pubmed:articleTitleBacterial signal peptide recognizes HeLa cell mitochondrial import receptors and functions as a mitochondrial leader sequence.lld:pubmed
pubmed-article:16041565pubmed:affiliationDepartment of Biochemistry, Purdue University, West Lafayette, Indiana 47907-2063, USA.lld:pubmed
pubmed-article:16041565pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:16041565pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:16041565pubmed:publicationTypeResearch Support, N.I.H., Extramurallld:pubmed
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