Abstract
In plants, mTERF proteins are primarily found in mitochondria and chloroplasts. Studies have identified several mTERF proteins that affect plant development, respond to abiotic stresses, and regulate organellar gene expression, but the functions and underlying mechanisms of plant mTERF proteins remain largely unknown. Here, we investigated the function of Arabidopsis mTERF27 using molecular genetic, cytological, and biochemical approaches. Arabidopsis mTERF27 had four mTERF motifs and was evolutionarily conserved from moss to higher plants. The phenotype of the mTERF27-knockout mutant mterf27 did not differ obviously from that of the wild-type under normal growth conditions but was hypersensitive to salt stress. mTERF27 was localized to the mitochondria, and the transcript levels of some mitochondrion-encoded genes were reduced in the mterf27 mutant. Importantly, loss of mTERF27 function led to developmental defects in the mitochondria under salt stress. Furthermore, mTERF27 formed homomers and directly interacted with multiple organellar RNA editing factor 8 (MORF8). Thus, our results indicated that mTERF27 is likely crucial for mitochondrial development under salt stress, and that this protein may be a member of the protein interaction network regulating mitochondrial gene expression.
Highlights
Mitochondria, which originated through the endosymbiosis of an α-proteobacterial ancestor, are considered the “power house” of the cell, providing the necessary energy for cellular function
Florescent localization analysis indicated that mTERF27-GFP signals overlapped well with the MitoTracker signal corresponding to mitochondria (Figure 1C)
Yeast growth on selective medium and bioluminescence signals produced by the catalysis of luciferin partly reflected that mTERF27 has weaker interaction with multiple organellar RNA editing factor 8 (MORF8), comparing with its homomer interaction
Summary
Mitochondria, which originated through the endosymbiosis of an α-proteobacterial ancestor, are considered the “power house” of the cell, providing the necessary energy for cellular function. The mitochondrial transcription termination factor (mTERF) protein family is a key player affecting gene expression in plastid and mitochondrial genomes [12]. Most mTERF proteins in plants target the mitochondria and chloroplasts, playing an active part in organellar gene expression and RNA transcription [14,25]. In addition to mTERFs, many other nuclear-encoded protein families, such as pentatricopeptide repeat (PPR) proteins and multiple organellar RNA editing factor (MORF). MORF deficiencies were shown to affect plant development and RNA editing at multiple sites in both mitochondria and plastids, many of which are associated with different individual PPR proteins [30,31,32]. We explored the direct interaction between mTERF27 and MORF8, and showed that mTERF27 interacted with itself to form homomers
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