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- W3169023314 abstract "Mitochondria play essential cellular roles that are highly dependent on proper regulation of mitochondrial gene expression. Mitochondrial dysfunction is associated with aging and several human diseases. The mterf family of proteins plays key roles regulating mitochondrial transcription and replication. We have solved the first crystal structure of a member of this family, human mterf1, bound in a sequence-specific manner to a 22-mer double stranded regulatory sequence. This 2.2A resolution structure reveals that the mterf proteins adopt a novel DNA binding fold allowing them to bind a relatively long sequence while partially melting the DNA duplex, a feature that is critical for stable binding. This unique binding mode provides insight into the molecular roles of the mterf proteins, explaining how they can positively and negatively modulate transcription. We have further investigated the mechanism of DNA binding through biochemical and structural analysis of different mterf mutants. In addition, our structural observations and equilibrium binding measurements suggest that a human pathogenic mitochondrial mutation that causes Kearns-Sayre syndrome (KSS), a neuromuscular disorder, interferes with binding of mterf1 to its main recognition sequence, implying that alterations in transcriptional regulation can lead to the development of this disease. This work was supported by NIH R00 ES015421." @default.
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- W3169023314 date "2010-04-01" @default.
- W3169023314 modified "2023-10-18" @default.
- W3169023314 title "A unique DNA binding mode enables human mterf1 to regulate mitochondrial transcription" @default.
- W3169023314 doi "https://doi.org/10.1096/fasebj.24.1_supplement.492.7" @default.
- W3169023314 hasPublicationYear "2010" @default.
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