Abstract
XPD (xeroderma pigmentosum group D) helicase serves as a prototype for 5’-3’ superfamily 2 helicases and has homologs in archaea, bacteria, and all eukaryotes. The helicase activity of eukaryotic XPD is vital to nucleotide excision repair (NER). In addition, some variants of XPD have been shown to have damage-sensing capabilities. In particular, mutation of specific residues in human XPD and in XPD from the archaeon Ferroplasma acidarmanus (FacXPD) compromises recognition of DNA damage in vivo and in vitro, respectively. However, many questions remain on XPD damage verification. Despite a number of studies, there is a lack of consensus on the mechanism by which XPD responds to different types of lesions or modifications and to the DNA strand they reside on. One study has suggested that distinct types of lesions are sensed through different mechanisms.
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