A chloroplastic inner envelope membrane protease is essential for plant development

Bölter, Bettina; Nada, Ahmed S.; Fulgosi, Hrovje; Soll, Jürgen

doi:10.1016/j.febslet.2005.12.098

Cited by 48 publications

(27 citation statements)

References 24 publications

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“…The mitochondrial enzyme is also the first RIP protease identified in plant mitochondria. Quite recently, another type of RIP protease which belongs to the S2P family was identified in plastids (Bolter et al 2006). Here, we showed that AtRBL12 does not cleave two known substrates of Pcp1, the yeast mitochondrial rhomboid.…”

Section: Discussionmentioning

confidence: 89%

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

et al. 2008

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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.

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Section: Discussionmentioning

confidence: 89%

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

et al. 2008

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“…RSEP1 belongs to the S2P family of membrane-bound metalloproteases, which includes At2g32480 in Arabidopsis that is localized to the inner chloroplast envelope membrane and required for chloroplast development (44). Orthologs of Arabidopsis At2g32480 are found in all plants, including Chlamydomonas (RSEP2) and other green algae.…”

Section: Resultsmentioning

confidence: 99%

Copper economy in Chlamydomonas : Prioritized allocation and reallocation of copper to respiration vs. photosynthesis

Kropat¹,

Gallaher²,

Urzica³

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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Inorganic elements, although required only in trace amounts, permit life and primary productivity because of their functions in catalysis. Every organism has a minimal requirement of each metal based on the intracellular abundance of proteins that use inorganic cofactors, but elemental sparing mechanisms can reduce this quota. A well-studied copper-sparing mechanism that operates in microalgae faced with copper deficiency is the replacement of the abundant copper protein plastocyanin with a heme-containing substitute, cytochrome (Cyt) c6. This switch, which is dependent on a copper-sensing transcription factor, copper response regulator 1 (CRR1), dramatically reduces the copper quota. We show here that in a situation of marginal copper availability, copper is preferentially allocated from plastocyanin, whose function is dispensable, to other more critical copper-dependent enzymes like Cyt oxidase and a ferroxidase. In the absence of an extracellular source, copper allocation to Cyt oxidase includes CRR1-dependent proteolysis of plastocyanin and quantitative recycling of the copper cofactor from plastocyanin to Cyt oxidase. Transcriptome profiling identifies a gene encoding a Zn-metalloprotease, as a candidate effecting copper recycling. One reason for the retention of genes encoding both plastocyanin and Cyt c6 in algal and cyanobacterial genomes might be because plastocyanin provides a competitive advantage in copper-depleted environments as a ready source of copper.

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“…Sequence analysis is consistent with thylakoid membrane localization. A related protein in Arabidopsis (albeit not an ortholog) is also organelle located (Bö lter et al, 2006). RSEP1 is therefore a prime candidate for degrading plastocyanin in copper deficiency.…”

Section: Backups and Copper Sparingmentioning

confidence: 99%

Systems Biology Approach in Chlamydomonas Reveals Connections between Copper Nutrition and Multiple Metabolic Steps

et al. 2011

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In this work, we query the Chlamydomonas reinhardtii copper regulon at a whole-genome level. Our RNA-Seq data simulation and analysis pipeline validated a 2-fold cutoff and 10 RPKM (reads per kilobase of mappable length per million mapped reads) (~1 mRNA per cell) to reveal 63 CRR1 targets plus another 86 copper-responsive genes. Proteomic and immunoblot analyses captured 25% of the corresponding proteins, whose abundance was also dependent on copper nutrition, validating transcriptional regulation as a major control mechanism for copper signaling in Chlamydomonas. The impact of copper deficiency on the expression of several O2-dependent enzymes included steps in lipid modification pathways. Quantitative lipid profiles indicated increased polyunsaturation of fatty acids on thylakoid membrane digalactosyldiglycerides, indicating a global impact of copper deficiency on the photosynthetic apparatus. Discovery of a putative plastid copper chaperone and a membrane protease in the thylakoid suggest a mechanism for blocking copper utilization in the chloroplast. We also found an example of copper sparing in the N assimilation pathway: the replacement of copper amine oxidase by a flavin-dependent backup enzyme. Forty percent of the targets are previously uncharacterized proteins, indicating considerable potential for new discovery in the biology of copper.

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A chloroplastic inner envelope membrane protease is essential for plant development

Cited by 48 publications

References 24 publications

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

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

Copper economy in Chlamydomonas : Prioritized allocation and reallocation of copper to respiration vs. photosynthesis

Systems Biology Approach in Chlamydomonas Reveals Connections between Copper Nutrition and Multiple Metabolic Steps

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