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

被引:71
作者
Schubot, FD [1 ]
Chen, CJ [1 ]
Rose, JP [1 ]
Dailey, TA [1 ]
Dailey, HA [1 ]
Wang, BC [1 ]
机构
[1] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
关键词
transcription factor; mitochondrial RNA polymerase; mtf1; mtTFB; mitochondrial transcription;
D O I
10.1110/ps.11201
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 Angstrom resolution. The protein consists of two domains, an N-terminal alpha/beta -domain and a smaller domain made up of four alpha -helices. Contrary to previous predictions, sc-mtTFB does not resemble Escherichia coli sigma -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.
引用
收藏
页码:1980 / 1988
页数:9
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