RT Journal Article
SR Electronic
T1 Protein aggregation in plant mitochondria inhibits translation and induces an NAC017-dependent ethylene-associated unfolded protein response
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2023.01.11.523570
DO 10.1101/2023.01.11.523570
A1 Song, Ce
A1 Li, Yuanyuan
A1 Hou, Yuqi
A1 Yang, Mengmeng
A1 Li, Tiantian
A1 Liu, Yinyin
A1 Xu, Chang
A1 Liu, Jinjian
A1 Millar, A. Harvey
A1 Wang, Ningning
A1 Li, Lei
YR 2023
UL http://biorxiv.org/content/early/2023/01/13/2023.01.11.523570.abstract
AB Loss of Lon1 in plant mitochondria led to stunted plant growth and accumulation of nuclear-encoded mitochondrial proteins, including Lon1 substrates, while mitochondrial-encoded proteins typically decreased in abundance. Lon1 mutants contained protein aggregates in the mitochondria matrix which were enriched in PPR-containing proteins and ribosomal subunits of the translation apparatus and were slowed in mitochondrial RNA splicing, editing and general translation rate. Transcriptome analysis showed multiple organellar unfolded protein responses involving ethylene biosynthesis were induced by either Lon1 loss, mitochondrial ribosomal protein loss, translation or respiratory inhibition and most were regulated by the mitochondrial retrograde signaling pathway dependent on the transcription factor NAC017. The short hypocotyl in lon1 mutants during skotomorphogenesis was partially rescued by ethylene inhibitors and mutants showed higher ethylene production rates than wildtype. Together this provides multiple steps in the link between loss of Lon1 and its whole plant phenotype.Single Sentence Summary Lon1 knockout inhibits mitochondrial-encoded gene translation and induces retrograde signaling involving unfolded protein responses.Competing Interest StatementThe authors have declared no competing interest.