Abstract
DNA-protein crosslinks (DPCs)-where proteins are covalently trapped on the DNA strand-block the progression of replication and transcription machineries and hence hamper the faithful transfer of genetic information. However, the repair mechanism of DPCs remains largely elusive. Here we have analyzed the roles of nucleotide excision repair (NER) and homologous recombination (HR) in the repair of DPCs both in vitro and in vivo using a bacterial system. Several lines of biochemical and genetic evidence show that both NER and HR commit to the repair or tolerance of DPCs, but differentially. NER repairs DPCs with crosslinked proteins of sizes less than 12-14 kDa, whereas oversized DPCs are processed exclusively by RecBCD-dependent HR. These results highlight how NER and HR are coordinated when cells need to deal with unusually bulky DNA lesions such as DPCs.
| Original language | English |
|---|---|
| Pages (from-to) | 147-158 |
| Number of pages | 12 |
| Journal | Molecular Cell |
| Volume | 28 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Oct 12 2007 |
| Externally published | Yes |
Fingerprint
Keywords
- DNA
- PROTEINS
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology
Cite this
Nucleotide Excision Repair and Homologous Recombination Systems Commit Differentially to the Repair of DNA-Protein Crosslinks. / Nakano, Toshiaki; Morishita, Soh; Katafuchi, Atsushi; Matsubara, Mayumi; Horikawa, Yusuke; Terato, Hiroaki; Salem, Amir M.H.; Izumi, Shunsuke; Pack, Seung Pil; Makino, Keisuke; Ide, Hiroshi.
In: Molecular Cell, Vol. 28, No. 1, 12.10.2007, p. 147-158.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Nucleotide Excision Repair and Homologous Recombination Systems Commit Differentially to the Repair of DNA-Protein Crosslinks
AU - Nakano, Toshiaki
AU - Morishita, Soh
AU - Katafuchi, Atsushi
AU - Matsubara, Mayumi
AU - Horikawa, Yusuke
AU - Terato, Hiroaki
AU - Salem, Amir M.H.
AU - Izumi, Shunsuke
AU - Pack, Seung Pil
AU - Makino, Keisuke
AU - Ide, Hiroshi
PY - 2007/10/12
Y1 - 2007/10/12
N2 - DNA-protein crosslinks (DPCs)-where proteins are covalently trapped on the DNA strand-block the progression of replication and transcription machineries and hence hamper the faithful transfer of genetic information. However, the repair mechanism of DPCs remains largely elusive. Here we have analyzed the roles of nucleotide excision repair (NER) and homologous recombination (HR) in the repair of DPCs both in vitro and in vivo using a bacterial system. Several lines of biochemical and genetic evidence show that both NER and HR commit to the repair or tolerance of DPCs, but differentially. NER repairs DPCs with crosslinked proteins of sizes less than 12-14 kDa, whereas oversized DPCs are processed exclusively by RecBCD-dependent HR. These results highlight how NER and HR are coordinated when cells need to deal with unusually bulky DNA lesions such as DPCs.
AB - DNA-protein crosslinks (DPCs)-where proteins are covalently trapped on the DNA strand-block the progression of replication and transcription machineries and hence hamper the faithful transfer of genetic information. However, the repair mechanism of DPCs remains largely elusive. Here we have analyzed the roles of nucleotide excision repair (NER) and homologous recombination (HR) in the repair of DPCs both in vitro and in vivo using a bacterial system. Several lines of biochemical and genetic evidence show that both NER and HR commit to the repair or tolerance of DPCs, but differentially. NER repairs DPCs with crosslinked proteins of sizes less than 12-14 kDa, whereas oversized DPCs are processed exclusively by RecBCD-dependent HR. These results highlight how NER and HR are coordinated when cells need to deal with unusually bulky DNA lesions such as DPCs.
KW - DNA
KW - PROTEINS
UR - http://www.scopus.com/inward/record.url?scp=34948826443&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=34948826443&partnerID=8YFLogxK
U2 - 10.1016/j.molcel.2007.07.029
DO - 10.1016/j.molcel.2007.07.029
M3 - Article
VL - 28
SP - 147
EP - 158
JO - Molecular Cell
JF - Molecular Cell
SN - 1097-2765
IS - 1
ER -