Characterization of the interaction between human cytochrome c and transfer RNAphe
Year: 2025
Type: article
Abstract: Cytochrome c (cyt c ) is released from mitochondria into the cytosol upon apoptotic stimulation, ultimately triggering programmed cell death. Recent studies have revealed that transfer RNA (tRNA) interacts with cyt c , impeding the formation of the apoptosome complex and thereby suppressing apoptosis. To elucidate the molecular mechanism underlying the interaction between cyt c and tRNA, nuclear magnetic resonance (NMR)-based chemical shift perturbation and intensity analysis were employed to characterize the binding interface between cyt c and tRNA phe . The findings demonstrate that cyt c primarily engages with tRNA phe through its 70-85 Ω-loop and N-terminal α-helix. This interaction sterically hinders the accessibility of small molecules, such as H 2 O 2 , to the hydrophobic pocket of cyt c , consequently attenuating its peroxidase activity. Furthermore, oxidative modification of cyt c , particularly the carbonylation of positively charged lysine residues, weakens this interaction.
Source: Magnetic Resonance Letters
Authors: Guangqing Zhang, Jianhua Zhan, Xin Chai, Bin Jiang, Maili Liu, Xu Zhang, Danyun Zeng
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: diamond
Funders: Innovative Research Group Project of the National Natural Science Foundation of China, Key Technologies Research and Development Program of Anhui Province, National Natural Science Foundation of China, Chinese Academy of Sciences, Natural Science Foundation of Hubei Province, National Key Research and Development Program of China
OpenAlex ID: W4410618500