Journal
NUCLEIC ACIDS RESEARCH
Volume 41, Issue 19, Pages 9183-9196Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkt664
Keywords
-
Categories
Funding
- European Molecular Biology Laboratory (EMBL), Heidelberg
Ask authors/readers for more resources
Transcription of tRNA-encoding genes by RNA polymerase (Pol) III requires the six-subunit general transcription factor IIIC that uses subcomplexes tau A and tau B to recognize two gene-internal promoter elements named A- and B-box. The Schizosaccharomyces pombe tau A subcomplex comprises subunits Sfc1, Sfc4 and Sfc7. The crystal structure of the Sfc1/Sfc7 heterodimer reveals similar domains and overall domain architecture to the Pol II-specific general transcription factor TFIIF Rap30/Rap74. The N-terminal Sfc1/Sfc7 dimerization module consists of a triple beta-barrel similar to the N-terminal TFIIF Rap30/Rap74 dimerization module, whereas the C-terminal Sfc1 DNA-binding domain contains a winged-helix domain most similar to the TFIIF Rap30 C-terminal winged-helix domain. Sfc1 DNA-binding domain recognizes single and double-stranded DNA by an unknown mechanism. Several features observed for A-box recognition by tau A resemble the recognition of promoters by bacterial RNA polymerase, where Sigma factor unfolds double-stranded DNA and stabilizes the non-coding DNA strand in an open conformation. Such a function has also been proposed for TFIIF, suggesting that the observed structural similarity between Sfc1/Sfc7 and TFIIF Rap30/Rap74 might also reflect similar functions.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available