Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 18, Issue 11, Pages 1281-U133Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2160
Keywords
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Funding
- Ministerio de Ciencia e Innovacion [BFU2006-09593, BFU2009-07134, BFU2008-02372, CSD2006-00023]
- Generalitat de Catalunya [SGR2009-1366, SGR2009-1309, SGR2009-1352]
- European Union [FP7-HEALTH-2010-261460, FP7-BioNMR-2010-261863]
- Instituto de Salud Carlos III [FIS-PI 10/00662]
- Consejo Superior de Investigaciones Cientificas
- MICINN
- Cusanswerk-Bischofliche Studienforderung
- Academy of Finland
- Tampere University Hospital
- Sigrid Juselius Foundation
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Human mitochondrial transcription factor A, TFAM, is essential for mitochondrial DNA packaging and maintenance and also has a crucial role in transcription. Crystallographic analysis of TFAM in complex with an oligonucleotide containing the mitochondrial light strand promoter (LSP) revealed two high-mobility group (HMG) protein domains that, through different DNA recognition properties, intercalate residues at two inverted DNA motifs. This induced an overall DNA bend of similar to 180 degrees, stabilized by the interdomain linker. This U-turn allows the TFAM C-terminal tail, which recruits the transcription machinery, to approach the initiation site, despite contacting a distant DNA sequence. We also ascertained that structured protein regions contacting DNA in the crystal were highly flexible in solution in the absence of DNA. Our data suggest that TFAM bends LSP to create an optimal DNA arrangement for transcriptional initiation while facilitating DNA compaction elsewhere in the genome.
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