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A mitochondrial prolyl aminopeptidase PAP2 releases N‐terminal proline and regulates proline homeostasis during stress response
Author(s) -
Ghifari Abi S.,
Teixeira Pedro F.,
Kmiec Beata,
Pružinská Adriana,
Glaser Elzbieta,
Murcha Monika W.
Publication year - 2020
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/tpj.14987
Subject(s) - proline , biochemistry , biology , aminopeptidase , cytosol , proline dehydrogenase , abiotic stress , amino acid , microbiology and biotechnology , enzyme , leucine , gene
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.