Abstract
TFIIS is a general transcription elongation factor that helps arrested RNA polymerase II elongation complexes resume transcription. We have previously shown that yeast TFIIS (yTFIIS) comprises three structural domains (I-III). The three-dimensional structures of domain II and part of domain III have been previously reported, but neither domain can autonomously stimulate transcription elongation. Here we report the NMR structural analysis of residues 131-309 of yTFIIS which retains full activity and contains all of domains II and III. We confirm that the structure of domain II in the context of fully active yTFIIS is the same as that determined previously for a shorter construct. We have determined the structure of the C-terminal zinc ribbon domain of active yTFIIS and shown that it is similar to that reported for a shorter construct of human TFIIS. The region linking domain II with the zinc ribbon of domain III appears to be conformationally flexible and does not adopt a single defined tertiary structure. NMR analysis of inactive mutants of yTFIIS support a role for the linker region in interactions with the transcription elongation complex.
Highlights
TFIIS is a general transcription elongation factor that helps arrested RNA polymerase II elongation complexes resume transcription
We have determined the structure of the C-terminal zinc ribbon domain of active yeast TFIIS (yTFIIS) and shown that it is similar to that reported for a shorter construct of human TFIIS
Solution structures have previously been reported for the three-helix bundle of domain II of yeast TFIIS [3] and the zinc ribbon of domain III of human TFIIS [9, 33]
Summary
TFIIS is a general transcription elongation factor that helps arrested RNA polymerase II elongation complexes resume transcription. We have determined the structure of the C-terminal zinc ribbon domain of active yTFIIS and shown that it is similar to that reported for a shorter construct of human TFIIS. The other class, includes TFIIS, its viral and archael sequence homologues, and the bacterial proteins, greA and greB These proteins do not affect the rate of nucleotide incorporation, but rather stimulate an activity in RNA polymerase II that enables it to transcribe throught blocks to elongation such as DNA-binding proteins, DNA-binding drugs, or particular sequences of DNA that promote transcription arrest [1]. The structures of yeast domain II and domain III of human TFIIS have been solved individually These proteins individually or in combination fail to stimulate transcription elongation. We wished to determine the structure of the 60-amino acid region that links the threehelix bundle of domain II with the zinc ribbon of domain III and determine the relative orientation, if any, of these two domains
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