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RECQ5/QE DNA Helicase Interacts with Retrotransposon mdg3 gag, an HIV Nucleocapsid-Related Protein
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- Nakayama Minoru
- Department of Biochemistry and Molecular Biology, Saitama University Cellular and Molecular Biology Laboratory, RIKEN
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- Quang Nguyen Duong
- Cellular and Molecular Biology Laboratory, RIKEN
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- Matsumoto Kouji
- Department of Biochemistry and Molecular Biology, Saitama University
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- Shibata Takehiko
- Cellular and Molecular Biology Laboratory, RIKEN
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- Ito Fumiaki
- Department of Biochemistry, Faculty of Pharmaceutical Sciences, Setsunan University
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- Kawasaki Katsumi
- Cellular and Molecular Biology Laboratory, RIKEN Department of Biochemistry, Faculty of Pharmaceutical Sciences, Setsunan University
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Description
Three hereditary human disorders, Werner's syndrome, Bloom's syndrome and a subset of Rothmund-Thomson syndrome, are associated with the loss of function of the respective RecQ homologues BLM, WRN, and RTS. These RecQ homologues are composed of a conserved helicase domain flanking C- and N-terminal domains. In contrast to BLM, WRN, and RTS, another RecQ homologue, RECQ5, possesses only short N-terminal region preceding the helicase domain and a long unique C-terminal domain. Although no disease has yet been genetically linked to a mutation in RECQ5, the prominent roles of RecQ helicase in the maintenance of genome stability suggest that RECQ5 helicase is likely to be important in vivo. To acquire a better understanding of RECQ5 function, we investigated protein interaction with the C-terminal domain of Drosophila melanogaster RECQ5/QE. A portion of Drosophila melanogaster retrotransposon mdg3, which corresponds to a nucleocapsid protein (gag-NC), was identified by use of the yeast two-hybrid system as interacting specifically with it. Glutathione S-transferase (GST) pull down experiments indicated that the mdg3 gag-NC bound mainly to an acidic region in the C-terminal domain of RECQ5/QE, which is adjacent to the RecQ helicase domain. The helicase activity of RECQ5/QE was stimulated by mdg3 gag-NC protein in vitro. These data suggest that RECQ5/QE helicase interacts physically and functionally with mdg3 gag-NC through the acidic region and that RecQ homologue might be involved in retrotransposition and genomic stability. <br>
Journal
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- Journal of Health Science
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Journal of Health Science 52 (1), 24-29, 2006
The Pharmaceutical Society of Japan
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Details 詳細情報について
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- CRID
- 1390001204498986624
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- NII Article ID
- 110006163210
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- NII Book ID
- AA11316464
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- ISSN
- 13475207
- 13449702
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- NDL BIB ID
- 7792911
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL Search
- Crossref
- CiNii Articles
- OpenAIRE
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- Abstract License Flag
- Disallowed