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Towards designer organelles by subverting the peroxisomal import pathway.

ABSTRACT: The development of 'designer' organelles could be a key strategy to enable foreign pathways to be efficiently controlled within eukaryotic biotechnology. A fundamental component of any such system will be the implementation of a bespoke protein import pathway that can selectively deliver constituent proteins to the new compartment in the presence of existing endogenous trafficking systems. Here we show that the protein-protein interactions that control the peroxisomal protein import pathway can be manipulated to create a pair of interacting partners that still support protein import in moss cells, but are orthogonal to the naturally occurring pathways. In addition to providing a valuable experimental tool to give new insights into peroxisomal protein import, the variant receptor-signal sequence pair forms the basis of a system in which normal peroxisomal function is downregulated and replaced with an alternative pathway, an essential first step in the creation of a designer organelle.Designer organelles could allow the isolation of synthetic biological pathways from endogenous components of the host cell. Here the authors engineer a peroxisomal protein import pathway orthogonal to the naturally occurring system.

SUBMITTER: Cross LL

PROVIDER: S-EPMC5587766 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature

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Towards designer organelles by subverting the peroxisomal import pathway.

Cross Laura L LL Paudyal Rupesh R Kamisugi Yasuko Y Berry Alan A Cuming Andrew C AC Baker Alison A Warriner Stuart L SL

Nature communications 20170906 1

The development of 'designer' organelles could be a key strategy to enable foreign pathways to be efficiently controlled within eukaryotic biotechnology. A fundamental component of any such system will be the implementation of a bespoke protein import pathway that can selectively deliver constituent proteins to the new compartment in the presence of existing endogenous trafficking systems. Here we show that the protein-protein interactions that control the peroxisomal protein import pathway can ...[more]

PMID: 28878206

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Project description:Dual targeting is a relatively little explored phenomenon by which some proteins are transported to two different subcellular compartments, such as chloroplasts and mitochondria. We previously showed that the R domain and the arm region of the melon necrotic spot virus coat protein could act as a dual-targeting peptide, which shares many relevant features in structure, amino acid composition, and functionality with that of the Thr-tRNA synthetases, the best-studied dual-targeted proteins by far. Here, we show that a viral coat protein hijacks the general pathways for organellar protein import and identifies the coat protein-interacting organellar translocon receptors. Our findings demonstrate for the first time that an exogenous dual-targeted protein uses the general Toc and Tom import systems to reach mitochondria and chloroplasts because it depends on the availability of NbToc75 and NbTom40. Interaction studies, subcellular localization analysis, and viral infection assays in silenced plants revealed the significance of plant receptors, such as the mitochondrion NbOm64 and chloroplast NbToc159A, in this transport. We also show that chloroplast protein translocation impairment could be interlinked with retrograde communication triggering a JA-based response that incidentally impairs viral infection. Future research may profit from our results to better comprehend cellular communication, protein import mechanisms, how preproteins interact with their receptors, and how plant pathogens manipulate host machinery to their ends. IMPORTANCE Many plant proteins and some proteins from plant pathogens are dually targeted to chloroplasts and mitochondria, and are supposed to be transported along the general pathways for organellar protein import, but this issue has not been explored yet. Moreover, organellar translocon receptors exist as families of several members whose functional specialization in different cargos is supposed but not thoroughly studied. This article provides novel insights into such topics showing for the first time that an exogenous protein, the melon necrotic spot virus coat protein, exploits the common Toc/Tom import systems to enter both mitochondria and chloroplasts while identifying the involved specific receptors.

Dataset Information

Towards designer organelles by subverting the peroxisomal import pathway.

Publications

Towards designer organelles by subverting the peroxisomal import pathway.

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