Binds to the mitochondrial light strand promoter and functions in mitochondrial transcription regulation (PubMed:29445193, PubMed:32183942). Component of the mitochondrial transcription initiation complex, composed at least of TFB2M, TFAM and POLRMT that is required for basal transcription of mitochondrial DNA (PubMed:29149603). In this complex, TFAM recruits POLRMT to a specific promoter whereas TFB2M induces structural changes in POLRMT to enable promoter opening and trapping of the DNA non-template strand (PubMed:20410300). Required for accurate and efficient promoter recognition by the mitochondrial RNA polymerase (PubMed:22037172). Promotes transcription initiation from the HSP1 and the light strand promoter by binding immediately upstream of transcriptional start sites (PubMed:22037172). Is able to unwind DNA (PubMed:22037172). Bends the mitochondrial light strand promoter DNA into a U-turn shape via its HMG boxes (PubMed:1737790). Required for maintenance of normal levels of mitochondrial DNA (PubMed:22841477, PubMed:19304746). May play a role in organizing and compacting mitochondrial DNA (PubMed:22037171). Monomer; binds DNA as a monomer (PubMed:19304746, PubMed:22037171, PubMed:22037172). Homodimer (PubMed:29149603). Component of the mitochondrial transcription initiation complex, composed at least of TFB2M, TFAM and POLRMT (PubMed:29149603). In this complex TFAM recruits POLRMT to the promoter whereas TFB2M induces structural changes in POLRMT to enable promoter opening and trapping of the DNA non-template strand (PubMed:29149603). Upon metabolic stress, forms a complex composed of FOXO3, SIRT3, TFAM and POLRMT (PubMed:29445193, PubMed:12897151). Interacts with TFB1M and TFB2M (PubMed:12897151). Interacts with CLPX; this enhances DNA-binding (PubMed:22841477). Binds DNA via its HMG boxes. When bound to the mitochondrial light strand promoter, bends DNA into a U-turn shape, each HMG box bending the DNA by 90 degrees. Phosphorylation by PKA within the HMG box 1 impairs DNA binding and promotes degradation by the AAA+ Lon protease. The disease is caused by variants affecting the gene represented in this entry.