Functional and physical interactions between ERCC1 and MSH2 complexes for resistance to cis-diamminedichloroplatinum(II) in mammalian cells

Lan, Li; Hayashi, Tsuyuko; Rabeya, Rokshana M.; Nakajima, Satoshi; Kanno, Shin Ichiro; Takao, Masashi; Matsunaga, Tsukasa; Yoshino, Masafumi; Ichikawa, Minoru; Riele, Hein te; Tsuchiya, Shigeru; Tanaka, Kiyoji; Yasui, Akira

doi:10.1016/j.dnarep.2003.10.005

Cited by 51 publications

(50 citation statements)

References 44 publications

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“…We have also shown that the recognition step by MutS␤ is stimulated by PCNA. Consistent with these biochemical findings, it has been shown that Msh2 and Ercc1-Xpf act cooperatively in human cells to remove cisplatin ICLs and that these proteins interact as determined by co-immunoprecipitation experiments (22). Furthermore, recent findings in budding yeast have implicated a role for Msh2 and Exo I in repair of nitrogen mustard ICLs (23).…”

supporting

confidence: 66%

The Pso4 mRNA Splicing and DNA Repair Complex Interacts with WRN for Processing of DNA Interstrand Cross-links

Zhang

Kaur

et al. 2005

Journal of Biological Chemistry

108

116

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DNA interstrand cross-links (ICLs) are perhaps the most formidable lesion encountered by the cellular DNA repair machinery, and the elucidation of the process by which they are removed in eukaryotic cells has proved a daunting task. In particular, the early stages of adduct recognition and uncoupling of the cross-link have remained elusive principally because genetic studies have not been highly revealing. We have developed a biochemical assay in which processing of a DNA substrate containing a site-specific psoralen ICL can be monitored in vitro. Using this assay we have shown previously that the mismatch repair factor MutS␤, the nucleotide excision repair heterodimer Ercc1-Xpf, and the replication proteins RPA and PCNA are involved in an early stage of psoralen ICL processing. Here, we report the identification of two additional factors required in the ICL repair process, a previously characterized pre-mRNA splicing complex composed of Pso4/Prp19, Cdc5L, Plrg1, and Spf27 (Pso4 complex), and WRN the protein deficient in Werner syndrome. Analysis of the WRN protein indicates that its DNA helicase function, but not its exonuclease activity, is required for ICL processing in vitro. In addition, we show that WRN and the Pso4 complex interact through a direct physical association between WRN and Cdc5L. A putative model for uncoupling of ICLs in mammalian cells is presented.

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supporting

confidence: 66%

The Pso4 mRNA Splicing and DNA Repair Complex Interacts with WRN for Processing of DNA Interstrand Cross-links

Zhang

Kaur

et al. 2005

Journal of Biological Chemistry

108

116

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“…A clear role for ERCC1-XPF in the uncoupling step has been established both in vitro and in vivo [20,21,25,[28][29][30][31], however, it is unlikely that this complex can carry out this step without the assistance of additional factors. We previously showed a requirement for the mismatch repair factor MutSβ in the early stage of ICL processing using an in vitro assay termed CRS (for cross-link induced repair synthesis) [21], and several other reports have demonstrated a role for mismatch repair components in ICL removal in vivo [26,27,32,33]. In addition, MSH2 and ERCC1-XPF have been shown to interact by co-IP experiments [26].…”

Section: Discussionmentioning

confidence: 95%

“…We previously showed a requirement for the mismatch repair factor MutSβ in the early stage of ICL processing using an in vitro assay termed CRS (for cross-link induced repair synthesis) [21], and several other reports have demonstrated a role for mismatch repair components in ICL removal in vivo [26,27,32,33]. In addition, MSH2 and ERCC1-XPF have been shown to interact by co-IP experiments [26]. We have also shown an involvement of RPA, WRN, and a four protein complex composed of PRP19/PSO4, CDC5L, SPF27, and PLRG1 in ICL repair processing using the CRS assay mentioned above [34].…”

Section: Discussionmentioning

confidence: 96%

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Double-strand breaks induce homologous recombinational repair of interstrand cross-links via cooperation of MSH2, ERCC1-XPF, REV3, and the Fanconi anemia pathway

Zhang

Liu

et al. 2007

DNA Repair

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DNA interstrand cross-linking agents have been widely used in chemotherapeutic treatment of cancer. The majority of interstrand cross-links (ICLs) in mammalian cells are removed via a complex process that involves the formation of double strand breaks at replication forks, incision of the ICL, and subsequent error-free repair by homologous recombination. How double strand breaks effect the removal of ICLs and the downstream homologous recombination process is not clear. Here, we describe a plasmid-based recombination assay in which one copy of the CFP gene is inactivated by a site-specific psoralen ICL and can be repaired by gene conversion with a mutated homologous donor sequence. We found that the homology dependent recombination (HDR) is inhibited by the ICL. However, when we introduced a double strand break adjacent to the site of the ICL, the removal of the ICL was enhanced and the substrate was funneled into a HDR repair pathway. This process was not dependent on the nucleotide excision repair pathway, but did require the ERCC1-XPF endonuclease and REV3. In addition, both the Fanconi anemia pathway and the mismatch repair protein MSH2 were required for the recombinational repair processing of the ICL. These results suggest that the juxtaposition of an ICL and a DSB stimulates repair of ICLs through a process requiring components of mismatch repair, ERCC1-XPF, REV3, Fanconi anemia proteins, and homologous recombination repair factors.

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“…73,74 Furthermore, XPF interacts with the FANC-A, Msh2, and non-erythroid α Spectrin αSPIIΣ proteins, further demonstrating its role in the removal of interstrand crosslinks. [75][76][77][78] A recently identified interesting role for XPF is its interaction with the telomere elongation factor TRF2. This factor is responsible for the conversion of telomeric TTAGGG repeats tracts to T-loop structures that protect the telomeres from inadvertent double-strand break repair.…”

Section: Cutting It Out: Xpg and Xpfmentioning

confidence: 99%

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Zou

Molecular Mechanisms of Xeroderma Pigmentosum

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Functional and physical interactions between ERCC1 and MSH2 complexes for resistance to cis-diamminedichloroplatinum(II) in mammalian cells

Cited by 51 publications

References 44 publications

The Pso4 mRNA Splicing and DNA Repair Complex Interacts with WRN for Processing of DNA Interstrand Cross-links

The Pso4 mRNA Splicing and DNA Repair Complex Interacts with WRN for Processing of DNA Interstrand Cross-links

Double-strand breaks induce homologous recombinational repair of interstrand cross-links via cooperation of MSH2, ERCC1-XPF, REV3, and the Fanconi anemia pathway

Other Proteins Interacting with XP Proteins

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