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• W47956346 abstract "Research Article1 December 1995free access The sorting signal of cytochrome b2 promotes early divergence from the general mitochondrial import pathway and restricts the unfoldase activity of matrix Hsp70. F. Gärtner F. Gärtner Biochemisches Institut, Universität Freiburg, Germany. Search for more papers by this author U. Bömer U. Bömer Biochemisches Institut, Universität Freiburg, Germany. Search for more papers by this author B. Guiard B. Guiard Biochemisches Institut, Universität Freiburg, Germany. Search for more papers by this author N. Pfanner N. Pfanner Biochemisches Institut, Universität Freiburg, Germany. Search for more papers by this author F. Gärtner F. Gärtner Biochemisches Institut, Universität Freiburg, Germany. Search for more papers by this author U. Bömer U. Bömer Biochemisches Institut, Universität Freiburg, Germany. Search for more papers by this author B. Guiard B. Guiard Biochemisches Institut, Universität Freiburg, Germany. Search for more papers by this author N. Pfanner N. Pfanner Biochemisches Institut, Universität Freiburg, Germany. Search for more papers by this author Author Information F. Gärtner1, U. Bömer1, B. Guiard1 and N. Pfanner1 1Biochemisches Institut, Universität Freiburg, Germany. The EMBO Journal (1995)14:6043-6057https://doi.org/10.1002/j.1460-2075.1995.tb00293.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Cytochrome b2 is imported into mitochondria and sorted to the intermembrane space by a bipartite N-terminal presequence, which is a matrix targeting sequenced followed by an intermembrane space sorting signal. The N-terminus of the mature protein forms a folded heme binding domain that depends on the unfoldase function of matrix (mt) Hsp70 for import. We report that the distance between the presequence and the heme binding domain is critical for the ability of mt-Hsp70 to promote import of the domain. Hybrid proteins with 40 or more amino acids between the presequence and the heme binding domain are arrested in the import machinery. The translocation arrest can be overcome by unfolding of the preprotein or by inactivation of the intermembrane space sorting signal. Moreover, the sorting signal prevents backsliding of the precursor polypeptide in the import site in the initial import step, when the signal has not made contact with the matrix. The results indicate that the sorting signal interacts with component(s) of the inner membrane/intermembrane space during the initial import step and promotes an early divergence of b2 preproteins from the general matrix import pathway, precluding an unfolding role for mt-Hsp70 in the translocation of most of the mature portions of a preprotein. We propose a sorting model of cytochrome b2 which explains the apparently divergent previous results by a unifying hypothesis. Previous ArticleNext Article Volume 14Issue 231 December 1995In this issue RelatedDetailsLoading ..." @default.
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• W47956346 title "The sorting signal of cytochrome b2 promotes early divergence from the general mitochondrial import pathway and restricts the unfoldase activity of matrix Hsp70." @default.
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• W47956346 doi "https://doi.org/10.1002/j.1460-2075.1995.tb00293.x" @default.
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