The Interaction Efficiency of XPD-p44 With Bulky DNA Damages Depends on the Structure of the Damage.
作者： Jochen Kuper , Rashid Anarbaev , Caroline Kisker , Irina Petruseva , Olga Lavrik
DOI: 10.3389/FCELL.2021.617160
关键词: Protein subunit 、 Hybridization probe 、 Helicase 、 Protein–DNA interaction 、 DNA 、 DNA damage 、 Transcription factor II H 、 Biophysics 、 Nucleotide excision repair 、 Chemistry
摘要: The successful elimination of bulky DNA damages via the nucleotide excision repair (NER) system is largely determined by damage recognition step. This step consists primary and verification damage. TFIIH helicase XPD plays a key role in during NER. To date, mechanism not sufficiently understood requires further detailed research. study systematic investigation interaction ctXPD (Chaetomium thermophilum) as well ctXPD-ctp44 with model DNAs, which contain structurally different lesions previously estimated NER efficiencies. We have used ATPase binding studies to assess damaged DNA. result analysis containing fluorescent photoactivatable demonstrates relationship between affinity for DNAs ability eliminate Photo-cross-linking probes repairable unrepairable reveals differences efficiency presence absence ctp44. In general, results obtained indicate interact suggest significant ctp44 subunit process.
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