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Crystal structure of the transcription factor sc-mtTFB offers insights into mitochondrial transcription

Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602, USA

Reprint requests to: B.-C. Wang, Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA e-mail: wang{at}bc11.bmb.uga.edu; fax: (706) 542-3077.

Although it is commonly accepted that binding of mitochondrial transcription factor sc-mtTFB to the mitochondrial RNA polymerase is required for specific transcription initiation in Saccharomyces cerevisiae, its precise role has remained undefined. In the present work, the crystal structure of sc-mtTFB has been determined to 2.6 Å resolution. The protein consists of two domains, an N-terminal /ß-domain and a smaller domain made up of four -helices. Contrary to previous predictions, sc-mtTFB does not resemble Escherichia coli -factors but rather is structurally homologous to rRNA methyltransferase ErmC'. This suggests that sc-mtTFB functions as an RNA-binding protein, an observation standing in contradiction to the existing model, which proposed a direct interaction of sc-mtTFB with the mitochondrial DNA promoter. Based on the structure, we propose that the promoter specificity region is located on the mitochondrial RNA polymerase and that binding of sc-mtTFB indirectly mediates interaction of the core enzyme with the promoter site.

Keywords: Transcription factor; mitochondrial RNA polymerase; mtf1; mtTFB; mitochondrial transcription

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