کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2185126 1095961 2011 11 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Targeting Capacity and Conservation of PreP Homologues Localization in Mitochondria of Different Species
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی بیولوژی سلول
پیش نمایش صفحه اول مقاله
Targeting Capacity and Conservation of PreP Homologues Localization in Mitochondria of Different Species
چکیده انگلیسی

Mitochondrial presequences and other unstructured peptides are degraded inside mitochondria by presequence proteases (PrePs) identified in Arabidopsis thaliana (AtPreP), humans (hPreP), and yeast (Cym1/Mop112). The presequences of A. thaliana and human PreP are predicted to consist of 85 and 29 amino acids, respectively, whereas the Saccharomyces cerevisiae Cym1/Mop112 presequence contains only 7 residues. These differences may explain the reported targeting of homologous proteins to different mitochondrial subcompartments. Here we have investigated the targeting capacity of the PreP homologues' presequences. We have produced fusion constructs containing N-terminal portions of AtPreP(1–125), hPreP(1–69), and Cym1(1–40) coupled to green fluorescent protein (GFP) and studied their import into isolated plant, mammalian, and yeast mitochondria, followed by mitochondrial subfractionation. Whereas the AtPreP presequence has the capacity to target GFP into the mitochondrial matrix of all three species, the hPreP presequence only targets GFP to the matrix of mammalian and yeast mitochondria. The Cym1/Mop112 presequence has an overall much weaker targeting capacity and only ensures mitochondrial sorting in its host species yeast. Revisiting the submitochondrial localization of Cym1 revealed that endogenous Cym1/Mop112 is localized to the matrix space, as has been previously reported for the plant and human homologues. Moreover, complementation studies in yeast show that native AtPreP restores the growth phenotype of yeast cells lacking Cym1, demonstrating functional conservation.

Graphical AbstractFigure optionsDownload high-quality image (174 K)Download as PowerPoint slideResearch Highlights
► PreP peptidasome degrades mitochondrial presequences and other unstructured peptides.
► PreP presequences in plant, mammals and yeast show different targeting capacity.
► In contrast to previous data we prove matrix localization of yeast PreP homologue.
► We demonstrate functional conservation of PreP homologues in different species.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Biology - Volume 410, Issue 3, 15 July 2011, Pages 400–410
نویسندگان
, , , , , , , , ,