論文

査読有り
2015年3月

A novel endonuclease that may be responsible for damaged DNA base repair in Pyrococcus furiosus

NUCLEIC ACIDS RESEARCH
  • Miyako Shiraishi
  • ,
  • Sonoko Ishino
  • ,
  • Takeshi Yamagami
  • ,
  • Yuriko Egashira
  • ,
  • Shinichi Kiyonari
  • ,
  • Yoshizumi Ishino

43
5
開始ページ
2853
終了ページ
2863
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1093/nar/gkv121
出版者・発行元
OXFORD UNIV PRESS

DNA is constantly damaged by endogenous and environmental influences. Deaminated adenine (hypoxanthine) tends to pair with cytosine and leads to the A:T -> G:C transition mutation during DNA replication. Endonuclease V (EndoV) hydrolyzes the second phosphodiester bond 3 ' from deoxyinosine in the DNA strand, and was considered to be responsible for hypoxanthine excision repair. However, the downstream pathway after EndoV cleavage remained unclear. The activity to cleave the phosphodiester bond 5 ' from deoxyinosine was detected in a Pyro-coccus furiosus cell extract. The protein encoded by PF1551, obtained from the mass spectrometry analysis of the purified fraction, exhibited the corresponding cleavage activity. A putative homolog from Thermococcus kodakarensis (TK0887) showed the same activity. Further biochemical analyses revealed that the purified PF1551 and TK0887 proteins recognize uracil, xanthine and the AP site, in addition to hypoxanthine. We named this endonuclease Endonuclease Q (EndoQ), as it may be involved in damaged base repair in the Thermococcals of Archaea.

リンク情報
DOI
https://doi.org/10.1093/nar/gkv121
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/25694513
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000352487100037&DestApp=WOS_CPL
ID情報
  • DOI : 10.1093/nar/gkv121
  • ISSN : 0305-1048
  • eISSN : 1362-4962
  • PubMed ID : 25694513
  • Web of Science ID : WOS:000352487100037

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