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Proposed mechanism for regulation of H 2 O 2 ‐induced programmed cell death in plants by binding of cytochrome c to 14‐3‐3 proteins
Author(s) -
ElenaReal Carlos A.,
GonzálezArzola Katiuska,
PérezMejías Gonzalo,
DíazQuintana Antonio,
VelázquezCampoy Adrián,
Desvoyes Bénédicte,
Gutiérrez Crisanto,
De la Rosa Miguel A.,
DíazMoreno Irene
Publication year - 2021
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.15146
Subject(s) - cytochrome c , biology , apoptosome , programmed cell death , microbiology and biotechnology , mitochondrion , cytochrome , apoptosis , cytosol , arabidopsis thaliana , caspase , biochemistry , coenzyme q – cytochrome c reductase , proteases , mutant , enzyme , gene
SUMMARY Programmed cell death (PCD) is crucial for development and homeostasis of all multicellular organisms. In human cells, the double role of extra‐mitochondrial cytochrome c in triggering apoptosis and inhibiting survival pathways is well reported. In plants, however, the specific role of cytochrome c upon release from the mitochondria remains in part veiled yet death stimuli do trigger cytochrome c translocation as well. Here, we identify an Arabidopsis thaliana 14‐3‐3ι isoform as a cytosolic cytochrome c target and inhibitor of caspase‐like activity. This finding establishes the 14‐3‐3ι protein as a relevant factor at the onset of plant H 2 O 2 ‐induced PCD. The in vivo and in vitro studies herein reported reveal that the interaction between cytochrome c and 14‐3‐3ι exhibits noticeable similarities with the complex formed by their human orthologues. Further analysis of the heterologous complexes between human and plant cytochrome c with plant 14‐3‐3ι and human 14‐3‐3ε isoforms corroborated common features. These results suggest that cytochrome c blocks p14‐3‐3ι so as to inhibit caspase‐like proteases, which in turn promote cell death upon H 2 O 2 treatment. Besides establishing common biochemical features between human and plant PCD, this work sheds light onto the signaling networks of plant cell death.