Background: Ssl1/p44 is a critical helicase stimulating factor for Rad3/XPD. Results: Structure-based mutation analysis of the β4-α5 loop of Ssl1/p44 resulted in defects of Rad3/XPD stimulation and yeast cell lethality. Conclusion: The β4-α5 loop of Ssl1/p44 is essential for the functional regulation of Rad3/XPD. Significance: These findings provide insights into the interaction between Rad3/XPD and Ssl1/p44 in TFIIH complex.
CITATION STYLE
Kim, J. S., Saint-André, C., Lim, H. S., Hwang, C. S., Egly, J. M., & Cho, Y. (2015). Crystal structure of the Rad3/XPD regulatory domain of Ssl1/p44. Journal of Biological Chemistry, 290(13), 8321–8330. https://doi.org/10.1074/jbc.M115.636514
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