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A mitochondrial prolyl aminopeptidase PAP2 releases N‐terminal proline and regulates proline homeostasis during stress response

Ghifari, Abi S. ; Teixeira, Pedro F. ; Kmiec, Beata ; Pružinská, Adriana ; Glaser, Elzbieta ; Murcha, Monika W.

The Plant journal : for cell and molecular biology, 2020-12, Vol.104 (5), p.1182-1194 [Periódico revisado por pares]

England: Blackwell Publishing Ltd

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  • Título:
    A mitochondrial prolyl aminopeptidase PAP2 releases N‐terminal proline and regulates proline homeostasis during stress response
  • Autor: Ghifari, Abi S. ; Teixeira, Pedro F. ; Kmiec, Beata ; Pružinská, Adriana ; Glaser, Elzbieta ; Murcha, Monika W.
  • Assuntos: Abiotic stress ; Amino acids ; Aminopeptidase ; Cytosol ; Homeostasis ; Mitochondria ; Peptides ; Pollen ; Proline ; Prolyl aminopeptidase ; Proteins ; Senescence ; Stresses
  • É parte de: The Plant journal : for cell and molecular biology, 2020-12, Vol.104 (5), p.1182-1194
  • Notas: ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
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  • Descrição: Amino acid recovery is the last step of organellar targeting peptide processing pathways, and prior studies have identified the metallo‐aminopeptidases responsible for the recovery of all amino acids from mitochondrial and chloroplastic targeting peptides, except for proline. This work characterises a proline‐specific aminopeptidase named proline aminopeptidase 2 (PAP2), identifying its activity, localisation and importance in maintaining proline homeostasis for normal plant development and during abiotic stress. Significance Statement Most mitochondrial proteins are synthesised in the cytosol and targeted into the organelle via N‐terminal targeting peptides that are cleaved upon import. The free targeting peptide is subsequently processed in a stepwise manner, with single amino acids released as final products. Here, we have characterised a proline‐cleaving aminopeptidase in Arabidopsis thaliana, prolyl aminopeptidase‐2 (PAP2, At3g61540). Activity assays show that PAP2 has a preferred activity to hydrolyse N‐terminal proline. Protein localisation studies revealed that PAP2 is exclusively targeted to mitochondria. Characterisation of pap2 mutants show defective pollen, enhanced dark‐induced senescence and increased susceptibility to abiotic stresses, which are likely attributed to a reduced level of accumulated free proline. Taken together, these results demonstrate the role of PAP2 in proline cleavage from mitochondrial peptides and proline homeostasis, which is required for the development of male gametophyte, tolerance to abiotic stresses, and leaf senescence.
  • Editor: England: Blackwell Publishing Ltd
  • Idioma: Inglês
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