Publication Information
Carrie et al., 2015
No external accession available
Abstract
J Exp Bot. 2015 May;66(9):2691-708. doi: 10.1093/jxb/erv064. Epub 2015 Mar 1.
Identification of cleavage sites and substrate proteins for two mitochondrial
intermediate peptidases in Arabidopsis thaliana.
Carrie C(1), Venne AS(2), Zahedi RP(2), Soll J(3).
Author information:
(1)Department of Biology I, Botany, Ludwig-Maximilians Universität München,
Großhaderner Strasse 2-4, D-82152 Planegg-Martinsried, Germany Carrie@lmu.de.
(2)Leibniz-Institut für Analytische Wissenschaften - ISAS - e.V., Otto-Hahn-Str.
11, D-44139 Dortmund, Germany.
(3)Department of Biology I, Botany, Ludwig-Maximilians Universität München,
Großhaderner Strasse 2-4, D-82152 Planegg-Martinsried, Germany Munich Centre for
Integrated Protein Science, CiPSM, Ludwig-Maximilians Universität München,
Feodor-Lynen-Strasse 25, D-81377 Munich, Germany.
Most mitochondrial proteins contain an N-terminal targeting signal that is
removed by specific proteases following import. In plant mitochondria, only
mitochondrial processing peptidase (MPP) has been characterized to date.
Therefore, we sought to determine the substrates and cleavage sites of the
Arabidopsis thaliana homologues to the yeast Icp55 and Oct1 proteins, using the
newly developed ChaFRADIC method for N-terminal protein sequencing. We
identified 88 and seven putative substrates for Arabidopsis ICP55 and OCT1,
respectively. It was determined that the Arabidopsis ICP55 contains an almost
identical cleavage site to that of Icp55 from yeast. However, it can also remove
a far greater range of amino acids. The OCT1 substrates from Arabidopsis
displayed no consensus cleavage motif, and do not contain the classical -10R
motif identified in other eukaryotes. Arabidopsis OCT1 can also cleave
presequences independently, without the prior cleavage of MPP. It was concluded
that while both OCT1 and ICP55 were probably acquired early on in the evolution
of mitochondria, their substrate profiles and cleavage sites have either
remained very similar or diverged completely.
© The Author 2015. Published by Oxford University Press on behalf of the Society
for Experimental Biology.
DOI: 10.1093/jxb/erv064
PMCID: PMC4986872
PMID: 25732537 [Indexed for MEDLINE]
