Processing of the presequence of the Schizosaccharomyces pombe Rieske iron-sulfur protein occurs in a single step and can be converted to two-step processing by mutation of a single proline to serine in the presequence.

The Journal of Biological Chemistry
J H NettBernard L Trumpower

Abstract

The iron-sulfur proteins of the cytochrome bc1 complexes of Schizosaccharomyces pombe and Saccharomyces cerevisiae contain the three amino acid motif RX( downward arrow)(F/L/I)XX(T/S/G)XXXX (downward arrow) that is typical for proteins that are cleaved sequentially in two steps by matrix processing peptidase (MPP) and mitochondrial intermediate peptidase (MIP). Despite the presence of this recognition sequence the S. pombe iron-sulfur protein is processed only once during import into mitochondria, whereas the S. cerevisiae protein is processed in two steps. Import of S. pombe iron-sulfur protein in which the putative MIP or MPP recognition sites are eliminated by site-directed mutagenesis and import of iron-sulfur protein into mitochondria from yeast mutants that lack MIP activity indicate that one step processing of the S. pombe iron-sulfur protein is independent of those sites and of MIP activity. Sequencing of the mature protein obtained after import in vitro and of the endogenous iron-sulfur protein isolated from mitochondrial membranes by preparative 2D-electrophoresis shows that MPP recognizes a second site in the presequence and processing occurs between residues 43 and 44. If proline-20 of the S. pombe presequence is ch...Continue Reading

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Citations

Jul 3, 2003·Proceedings of the National Academy of Sciences of the United States of America·Pawel GolikJaga Lazowska
Aug 23, 2002·Biochimica Et Biophysica Acta·Oleksandr GakhGrazia Isaya
Oct 25, 2011·Molecular Cell·Nikola WagenerWalter Neupert
Aug 1, 2018·Molecular and Cellular Biology·Olga Zurita Rendón, Eric A Shoubridge
Apr 4, 2001·The Journal of Biological Chemistry·S F ShihJ Y Lin
Oct 16, 2002·The Journal of Biological Chemistry·Emma Berta Gutierrez-CirlosBernard L Trumpower

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