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1 H, 13 C and 15 N resonance assignments of TFIIS LW domain from Saccharomyces cerevisiae.

Jie GaoJiahai ZhangXiaoming TuShanhui Liao
Published in: Biomolecular NMR assignments (2022)
TFIIS is one of the best-characterized transcription elongation factors, with a domain I (named also as LW domain) in the N-terminus. It can relieve the arrest of RNA polymerase II (RNAP II) when the elongation of RNAP II is impaired. Here we report the resonance assignments of the protein backbone and side chains of the LW domain of TFIIS from S. cerevisiae, the secondary structure prediction indicates the ScTFIIS LW domain contains six α-helices with no β-sheet, which will lay the foundation for the protein structure determination and function elucidation.
Keyphrases
  • saccharomyces cerevisiae
  • energy transfer
  • transcription factor
  • protein protein
  • cell cycle
  • high resolution
  • mass spectrometry
  • small molecule