Structural analysis and DNA binding of the HMG domains of the human mitochondrial transcription factor A

Gangelhoff, Todd A.; Mungalachetty, Purnima S.; Nix, Jay C.; Churchill, Mair E.  A.

doi:10.1093/nar/gkp157

Title: Structural analysis and DNA binding of the HMG domains of the human mitochondrial transcription factor A

Journal Article · Fri Mar 20 00:00:00 EDT 2009 · Nucleic Acids Research

DOI:https://doi.org/10.1093/nar/gkp157· OSTI ID:1625461

Gangelhoff, Todd A. ^[1]; Mungalachetty, Purnima S. ^[2]; Nix, Jay C. ^[3]; Churchill, Mair E. A. ^[1]

Univ. of Colorado, Denver, CO (United States). Dept. of Pharmacology; Univ. of Colorado, Denver, CO (United States). Molecular Biology Program
Univ. of Colorado, Denver, CO (United States). Dept. of Pharmacology
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Advanced Light Source (ALS). Molecular Biology Consortium. Beamline 4.2.2

The mitochondrial transcription factor A (mtTFA) is central to assembly and initiation of the mitochondrial transcription complex. Human mtTFA (h-mtTFA) is a dual high mobility group box (HMGB) protein that binds site-specifically to the mitochondrial genome and demarcates the promoters for recruitment of h-mtTFB1, h-mtTFB2 and the mitochondrial RNA polymerase. The stoichiometry of h-mtTFA was found to be a monomer in the absence of DNA, whereas it formed a dimer in the complex with the light strand promoter (LSP) DNA. Each of the HMG boxes and the C-terminal tail were evaluated for their ability to bind to the LSP DNA. Removal of the C-terminal tail only slightly decreased nonsequence specific DNA binding, and box A, but not box B, was capable of binding to the LSP DNA. The X-ray crystal structure of h-mtTFA box B, at 1.35 Å resolution, revealed the features of a noncanonical HMG box. Interactions of box B with other regions of h-mtTFA were observed. Together, these results provide an explanation for the unusual DNA-binding properties of box B and suggest possible roles for this domain in transcription complex assembly.

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Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1625461

Journal Information:: Nucleic Acids Research, Vol. 37, Issue 10; ISSN 0305-1048

Publisher:: Oxford University PressCopyright Statement

Country of Publication:: United States

Language:: English

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