Crystallization and preliminary X-ray diffraction analysis of the mitochondrial transcription factor sc-mtTFB from<i>Saccharomyces cerevisiae</i>

Schubot, Florian D.; Chen, Chun‐Jung; Rose, John P.; Wang, Bi-Cheng

doi:10.1107/s0907444900005060

Cited by 2 publications

(1 citation statement)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Details of the cloning, expression, purification, and crystallization of sc‐mtTFB are published elsewhere (Schubot et al 2000). Initial X‐ray diffraction data collection on the native and xenon (Xe)‐derivative crystals was performed on a Rigaku R‐Axis IV area detector at −170°C.…”

Section: Methodsmentioning

confidence: 99%

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

et al. 2001

Self Cite

View full text Add to dashboard Cite

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 ␣/␤-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.

show abstract

Section: Methodsmentioning

confidence: 99%