A human transcription factor in search mode.
Stony Brook, United States. In Nucleic Acids Res, Feb 2016
Here, we investigate the conformational switch of the human mitochondrial transcription termination factor MTERF1, which has a modular, superhelical topology complementary to DNA.
Nucleic acid recognition by tandem helical repeats.
Nashville, United States. In Curr Opin Struct Biol, 2012
Unlike DNA sequence recognition motifs that rely mainly on major groove read-out, MTERF and ALK motifs locate target sequences and aberrant nucleotides within DNA by resculpting the double-helix through extensive backbone contacts.
Mitochondrial transcription: how does it end?
Stony Brook, United States. In Transcription, 2011
Studies indicate that the structure of the mitochondrial transcription termination factor (MTERF1) provides insight into the mechanism of binding, recognition of the termination sequence and the conformational changes involved in mediating termination.
MTERF1 gives mtDNA an unusual twist.
Göteborg, Sweden. In Cell Metab, 2010
Recent work in Cell (Yakubovskaya et al., 2010) reports a novel DNA-binding fold in mitochondrial transcription termination factor 1 (MTERF1), which causes unwinding and base eversion at its target mtDNA sequence.