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Xeroderma pigmentosum group C protein complex is the initiator of global genome nucleotide excision repair.
TLDR
A novel DNA damage recognition-competition assay is used to identify XPC-HR23B as the earliest damage detector to initiate NER: it acts before the known damage-binding protein XPA, providing a plausible explanation for the extreme damage specificity exhibited by global genome repair. Expand
UV-Induced Ubiquitylation of XPC Protein Mediated by UV-DDB-Ubiquitin Ligase Complex
TLDR
It is shown that XPC undergoes reversible ubiquitylation upon UV irradiation of cells and that this depends on the presence of functional UV-DDB activity, which strongly suggest that ubiquitylated plays a critical role in the transfer of the UV-induced lesion from UV- DDB to XPC. Expand
The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase η
TLDR
Recombinant human DNA polymerase η corrects the inability of XP-V cell extracts to carry out DNA replication by bypassing thymine dimers on damaged DNA, indicating that DNA polymerases η could be the XPV gene product. Expand
Structural Basis of UV DNA-Damage Recognition by the DDB1–DDB2 Complex
TLDR
The structure provides insights into damage recognition in chromatin and suggests a mechanism by which the DDB1-associated CUL4 ubiquitin ligase targets proteins surrounding the site of damage. Expand
A multistep damage recognition mechanism for global genomic nucleotide excision repair.
TLDR
A highly sensitive gel mobility shift assay revealed that XPC-HR23B specifically binds a small bubble structure with or without damaged bases, whereas dual incision takes place only when damage is present in the bubble, evidence that damage recognition for NER is accomplished through at least two steps. Expand
The Molecular Basis of CRL4DDB2/CSA Ubiquitin Ligase Architecture, Targeting, and Activation
TLDR
The data support a general mechanism of ligase activation, which is induced by CSN displacement from CRL4(DCAF) on substrate binding to the DCAF, and indicates that the mobility of the ligase arm creates a defined ubiquitination zone around the damage, which precludes direct ligaseactivation by DNA lesions. Expand
Xeroderma pigmentosum variant (XP‐V) correcting protein from HeLa cells has a thymine dimer bypass DNA polymerase activity
TLDR
A sensitive assay system is established using an SV40 origin‐based plasmid to detect XP‐V complementation activity and isolated a protein from HeLa cells capable of complementing the defects inXP‐V cell extracts that corrected the translesion defects of extracts from three XPV cell strains. Expand
Centrin 2 Stimulates Nucleotide Excision Repair by Interacting with Xeroderma Pigmentosum Group C Protein
TLDR
Centrin 2 enhanced the cell-free NER dual incision and damaged DNA binding activities of XPC, which likely require physical interaction between XPC and centrin 2. Expand
High‐efficiency bypass of DNA damage by human DNA polymerase Q
TLDR
It is found that POLQ has an exceptional ability to bypass an AP site, inserting A with 22% of the efficiency of a normal template, and continuing extension as avidly as with a normally paired base. Expand
Human DNA Polymerase N (POLN) Is a Low Fidelity Enzyme Capable of Error-free Bypass of 5S-Thymine Glycol*
TLDR
The first purification of the recombinant enzyme and examination of its biochemical properties, as a step toward understanding the functions of POLN, found it to be particularly adept at efficient and accurate translesion synthesis past a 5S-thymine glycol. Expand
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