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Significance All eukaryotes respond to DNA damage by polyubiquitylation and degradation of the largest subunit of RNA polymerase II (pol II), facilitated by the Elongin-Cullin ubiquitin ligase. In yeast, the recruitment of the ubiquitin ligase to pol II is dependent on Def1. We report a finding made in the course of isolating TFIIH-Def1 from yeast that suggests a potential novel function of Def1 as a transcription regulator in response to cellular stress. The function of Def1 in transcription regulation is demonstrably separable from its role in coordinating pol II stability in response to cellular stress.
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Damodaren et al. (2017) studied this question.
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