Plant mitochondrial rhomboid, AtRBL12, has different substrate specificity from its yeast counterpart

Beata Kmiec-Wisniewska, Katrin Krumpe, Adam Urantowka, Wataru Sakamoto, Elke Pratje, Hanna Janska

Research output: Contribution to journalArticlepeer-review

37 Citations (Scopus)


Rhomboid proteins comprise a class of serine proteases that are conserved in all kingdoms of organisms. They contain six or seven transmembrane helices and control a wide range of cellular functions and developmental processes by intramembrane proteolysis. This paper provides experimental evidence for the existence of rhomboid proteases in plant mitochondria and chloroplasts. Among 15 putative rhomboid-like proteins in Arabidopsis thaliana, we selected five predicted as mitochondrially targeted. For these proteins we performed the GFP transient assay, and identified two homologues, AtRBL11 (At5g25752) and AtRBL12 (At1g18600) to be targeted into plastids and mitochondria, respectively. Phylogenetic analysis reveals that AtRBL12 or AtRBL11 have only one clear orthologue in plant species with completely sequenced genomes. Complementation of the yeast lacking a functional copy of mitochondrial rhomboid with AtRBL12 indicates that this plant protease, in contrast to the human orthologue, does not recognize the yeast substrates, cytochrome c peroxidase (Ccp1) or dynamin-like GTPase (Mgm1). In agreement with this, we did not observe processing of Mgm1 when labeled precursor of this protein was incubated in vitro with Arabidopsis mitochondrial extract. Our results imply that plant mitochondrial rhomboids function in a specific manner and thus differ from their yeast and mammal counterparts.

Original languageEnglish
Pages (from-to)159-171
Number of pages13
JournalPlant Molecular Biology
Issue number1-2
Publication statusPublished - Sept 2008


  • AtRBL12
  • Intramembrane proteolysis
  • Pcp1
  • Plant mitochondria
  • Rhomboid proteases

ASJC Scopus subject areas

  • Agronomy and Crop Science
  • Genetics
  • Plant Science


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