His-87 ligand in mitoNEET is crucial for the transfer of iron sulfur clusters from mitochondria to cytosolic aconitase

• Published in: Biochemical and biophysical research communications Vol. 470; no. 1; pp. 226 - 232
• Main Authors: Tan, Guoqiang, Liu, Danhui, Pan, Feiyan, Zhao, Jin, Li, Tang, Ma, Yin, Shen, Bo, Lyu, Jianxin
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 29.01.2016
• Subjects: Aconitase; Aconitate Hydratase - metabolism; Binding Sites; Biological Transport, Active - physiology; Cytosol - metabolism; Hep G2 Cells; His-87 ligand mutations; Histidine - chemistry; Histidine - metabolism; Humans; Iron-sulfur cluster; Iron-Sulfur Proteins - metabolism; MCF-7 Cells; Mitochondria - metabolism; Mitochondrial Proteins - chemistry; Mitochondrial Proteins - metabolism; MitoNEET; Protein Binding; Iron-sulfur cluster; Aconitase; MitoNEET; His-87 ligand mutations
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2016.01.040

MitoNEET is the first identified iron sulfur protein that located in the mitochondrial outer membrane. We showed that knockdown of mitoNEET did not affect the iron sulfur protein expression in mitochondria and cytoplasm, but significantly reduced the cytosolic aconitase activity. The reduction of aconitase activity was rescued by transfection of wild type mitoNEET, but not by mitoNEET mutants H87C and H87S. Our results confirm the observation that mitoNEET is important in transferring the iron sulfur clusters to the cytosolic aconitase in living cells and the His-87 ligand in mitoNEET plays important role in this process.