Characterization of the sea urchin mitochondrial transcription factor A reveals unusual features

• Published in: Mitochondrion Vol. 14; no. 1; pp. 34 - 41
• Main Authors: Deceglie, Stefania, Lionetti, Claudia, Stewart, James B, Habermann, Bianca, Roberti, Marina, Cantatore, Palmiro, Loguercio Polosa, Paola
• Format: Journal Article
• Language: English
• Published: Netherlands 01.01.2014
• Subjects: Amino Acid Sequence; Animals; Binding Sites; DNA Footprinting; DNA, Mitochondrial - metabolism; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - genetics; DNA-Binding Proteins - metabolism; Genetic Variation; Mitochondrial Proteins - chemistry; Mitochondrial Proteins - genetics; Mitochondrial Proteins - metabolism; Models, Molecular; Molecular Sequence Data; Protein Binding; Protein Conformation; Sea Urchins - genetics; Transcription Factors - chemistry; Transcription Factors - genetics; Transcription Factors - metabolism; TFAM; Mitochondria; Sea urchin; DNA binding; mtDNA transcription
• ISSN: 1567-7249; 1872-8278
• DOI: 10.1016/j.mito.2013.10.003

Sea urchin mtDNA is transcribed via a different mechanism compared to vertebrates. To gain information on the apparatus of sea urchin mitochondrial transcription we have characterized the DNA binding properties of the mitochondrial transcription factor A (TFAM). The protein contains two HMG box domains but, differently from vertebrates, displays a very short C-terminal tail. Phylogenetic analysis showed that the distribution of tail length is mixed in the different lineages, indicating that it is a trait that undergoes rapid changes during evolution. Homology modeling suggests that the protein adopts the same configuration of the human counterpart and possibly a similar mode of binding to DNA. DNase I footprinting showed that TFAM specifically contacts mtDNA at a fixed distance from three AT-rich consensus sequences that were supposed to act as transcriptional initiation sites. Bound sequences are homologous and contain an inverted repeat motif, which resembles that involved in the intercalation of human TFAM in LSP DNA. The here reported data indicate that sea urchin TFAM specifically binds mtDNA. The protein could intercalate residues at the DNA inverted motif and, despite its short tail, might have a role in mitochondrial transcription.