Respiratory Complexes III and IV Can Each Bind Two Molecules of Cytochrome c at Low Ionic Strength
The transient interactions of respiratory cytochrome c with complexes III and IV is herein investigated by using heterologous proteins, namely human cytochrome c, the soluble domain of plant cytochrome c1 and bovine cytochrome c oxidase. The binding molecular...
Cytochrome c1 exhibits two binding sites for cytochrome c in plants
In plants, channeling of cytochrome c molecules between complexes III and IV has been purported to shuttle electrons within the supercomplexes instead of carrying electrons by random diffusion across the intermembrane bulk phase. However, the mode plant cytochrome c...
Oxidative stress contributes to autophagy induction in response to endoplasmic reticulum stress in Chlamydomonas
The accumulation of unfolded/misfolded proteins in the endoplasmic reticulum (ER) results in the activation of stress responses such as the unfolded protein response or the catabolic process of autophagy to ultimately recover cellular homeostasis. ER stress also...
The binding of TIA-1 to RNA C-rich sequences is driven by its C-terminal RRM domain
T-cell intracellular antigen-1 (TIA-1) is a key DNA/RNA binding protein that regulates translation by sequestering target mRNAs in stress granules (SG) in response to stress conditions. TIA-1 possesses three RNA recognition motifs (RRM) along with a glutamine-rich...