Solution structure of the voltage-gated Tim23 channel in complex with a mitochondrial presequence peptide
Dear Editor,
Most mitochondrial proteins are synthesized in the cytosol and transported into various mitochondrial subcompartments in a process that is mediated by intricate multimeric machineries.Tim23,the key component of the TIM23 complex forming a channel in the mitochondrial inner membrane (MIM),is believed to recognize and translocate precursor proteins into the mitochondrial matrix or to release them into the MIM.1 Previous study has demonstrated that purified Tim23 forms a protein-conducting channel that can be activated by an appropriate change in the membrane potential in the presence of a mimetic mitochondrial preprotein,2 a signaling peptide corresponding to the presequence of cytochrome c oxidase subunit V (denoted as pCoxlV,primary sequence:MLSLRQSIRFFKPATRTLCSSRYLL).Here,we present the three-dimensional (3D) solution structure of the yeast Tim23 channel in complex with pCoxlV in micelles as determined by high-resolution nuclear magnetic resonance(NMR),providing structural insight into the molecular mechanism of presequence translocation.
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We acknowledge the High Magnetic Field Laboratory of Chinese Academy of Sciences and the Biomolecular Magnetic Resonance Center supported by Hesse State at University of Frankfurt for allowing us to access NMR spectrometers;A portion of this work was supported by the High Magnetic Field Laboratory of Anhui Province;This study was supported by grants from the Ministry of Science and Technology of ChinaGrant No,,2016YFA0400901,the National Natural Science Foundation of ChinaGrant No,,U1632274,Hefei Science Center of Chinese Academy of Sciences Grant No,,2020HSC-CIP011 and by iNEXT-Discovery,project n
2021-08-04（万方平台首次上网日期，不代表论文的发表时间）
共4页
821-824
