RETRACTED ARTICLE: Human MTERF3 crystal structure forms a left-handed superhelix

Abstract

The mitochondrial transcription termination factors (MTERFs) play an important role in the transcriptional regulation of mitochondrial genes. In mammals, the MTERF1-4 protein subfamilies contain all of the mTERF domains needed to interact with mitochondrial DNA (mtDNA). To understand the molecular function of these domains, we solved the crystal structure of MTERF3 at 2.71-Å resolution, which forms a left-handed superhelix with a half-donut shape. In addition, we performed structural modeling of the MTERF3 and mtDNA complex. The positive charged concave region in the center of the MTERF3 structure suggests this region might be the mtDNA binding interface to accommodate the mtDNA helix. In comparison to the DNA-bound MTERF1 structure, our DNA-bound MTERF3 model suggests that MTERF3 has a different DNA-binding conformation than MTERF1, which is consistent with the different transcriptional functions of these two proteins.