The protein shuffle

@article{Park2006ThePS,
  title={The protein shuffle},
  author={Chin-Ju Park and Byong-Seok Choi},
  journal={The FEBS Journal},
  year={2006},
  volume={273}
}
Xeroderma pigmentosum (XP) is an inherited disease in which cells from patients exhibit defects in nucleotide excision repair (NER). XP proteins A–G are crucial in the processes of DNA damage recognition and incision, and patients with XP can carry mutations in any of the genes that specify these proteins. In mammalian cells, NER is a dynamic process in which a variety of proteins interact with one another, via modular domains, to carry out their functions. XP proteins are key players in… 
Other proteins interacting with XP proteins.
  • S. Shell, Y. Zou
  • Biology
    Advances in experimental medicine and biology
  • 2008
TLDR
This chapter describes these proteins and their interactions and discusses their effects on the XP proteins, DNA repair, and genome stability.
Redefining the DNA-Binding Domain of Human XPA
TLDR
It is demonstrated using a fluorescence anisotropy DNA-binding assay that the previously reported XPA DBD binds DNA with substantially weaker affinity than the full-length protein, and XPA98–239 is a suitable model to examine the DNA binding activity of human XPA.
A new structural insight into XPA–DNA interactions
TLDR
A novel structure-function view of XPA–DNA junction interactions is provided, showing that XPA physically interacts with the DNA junctions via two lysines located in the previously known XPA(98–219) DBD (DNA-binding domain) and uncovered new lysine residues involved in the binding.
Role of interaction of XPF with RPA in nucleotide excision repair.
Effect of point substitutions within the minimal DNA-binding domain of xeroderma pigmentosum group a protein on interaction with DNA intermediates of nucleotide excision repair
TLDR
No direct correlation between DNA binding and activity in NER for these XPA mutants is suggested, with the difference between protein affinities to different DNA structures increasing as DNA binding activity of the mutant decreased.
Mouse models for xeroderma pigmentosum group A and group C show divergent cancer phenotypes.
TLDR
It is believed that XPC plays a role in the removal of oxidative DNA damage and that Xpc(-/-) mice display a significant increase in lung tumors and a significant elevation in mutant frequency in lung, and Xpc-deficient MEFs show greater sensitivity to oxygen when compared with Xpa (-/-) and wild-type mice.
Dynamics of nucleotide excision repair complex assembly and disassembly in vivo
TLDR
The data presented present a comprehensive view of the in vivo behaviour of a protein that is involved in a complex chromatin associated process, as well as creating mammalian cell lines that lack functional endogenous XPG and stably express EGFP-tagged XPG.
DNA repair pathways and hereditary cancer susceptibility syndromes.
TLDR
Though patients with identifiable cancer predisposition syndromes are rare, defining their molecular defects has led to widespread applicability by uncovering relevant molecular pathways that are perturbed via somatic mutations in the majority of sporadic cancers.
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References

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The Xeroderma Pigmentosum Group C Protein Complex XPC-HR23B Plays an Important Role in the Recruitment of Transcription Factor IIH to Damaged DNA*
TLDR
It is demonstrated that XPC-HR23B interacts with general transcription factor IIH (TFIIH) both in vivo and in vitro and plays a crucial role in the recruitment of TFIIH to damaged DNA in global genome repair.
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.
Identification of a damaged-DNA binding domain of the XPA protein.
Structure of the XPC binding domain of hHR23A reveals hydrophobic patches for protein interaction
TLDR
The interaction of the XPC binding domain (XPCB) of h HR23A/B with XPC protein has been shown to be important for its optimal function in NER and the solution structure of XPCB of hHR23A is determined.
Formation of a ternary complex by human XPA, ERCC1, and ERCC4(XPF) excision repair proteins.
  • C. Park, A. Sancar
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1994
TLDR
The XPA damage recognition protein makes a ternary complex with the ERCC1/ERCC4(XPF) heterodimer with a potential nuclease function that complemented cell-free extracts of excision repair cross-complementing 1 (ERCC-1), ERCC-4 (XP-F), and XP-A mutants.
Strong Functional Interactions of TFIIH with XPC and XPG in Human DNA Nucleotide Excision Repair, without a Preassembled Repairosome
TLDR
The strongest interaction was between TFIIH and XPC-HR23B, indicating a coupled role of these proteins in early steps of repair, and no evidence for a repair complex that contained all of the NER components.
DNA repair factor XPC is modified by SUMO-1 and ubiquitin following UV irradiation
TLDR
It is concluded that XPC protein is modified by SUMO-1 and ubiquitin following UV irradiation and these modifications require the functions of DDB2 and XPA, as well as the Ubiquitin–proteasome system.
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