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 journalArticle

32 Citations (Scopus)

Abstract

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
Volume68
Issue number1-2
DOIs
Publication statusPublished - Sep 2008

Fingerprint

substrate specificity
Substrate Specificity
Yeast
Mitochondria
Yeasts
yeasts
Peptide Hydrolases
Substrates
Cytochrome-c Peroxidase
Proteolysis
Dynamins
cytochrome-c peroxidase
Proteins
mitochondria
Mammals
Protein Precursors
proteinases
proteins
GTP Phosphohydrolases
Serine Proteases

Keywords

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

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

Cite this

Plant mitochondrial rhomboid, AtRBL12, has different substrate specificity from its yeast counterpart. / Kmiec-Wisniewska, Beata; Krumpe, Katrin; Urantowka, Adam; Sakamoto, Wataru; Pratje, Elke; Janska, Hanna.

In: Plant Molecular Biology, Vol. 68, No. 1-2, 09.2008, p. 159-171.

Research output: Contribution to journalArticle

Kmiec-Wisniewska, Beata ; Krumpe, Katrin ; Urantowka, Adam ; Sakamoto, Wataru ; Pratje, Elke ; Janska, Hanna. / Plant mitochondrial rhomboid, AtRBL12, has different substrate specificity from its yeast counterpart. In: Plant Molecular Biology. 2008 ; Vol. 68, No. 1-2. pp. 159-171.
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