Altered DNA Binding by the Human Rad51-R150Q Mutant Found in Breast Cancer Patients(Biochemistry)

スポンサーリンク

概要

• 論文の詳細を見る

• The human Rad51 protein (HsRad51) catalyzes homologous pairing and strand exchange between single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA) during recombinational repair of double-stranded DNA breaks. An HsRad51 mutation that results in the substitution of Gin for Arg150 (R150Q) was found in bilateral breast cancer patients; however, the consequences of this R150Q mutation have not been elucidated. To determine how this HsRad51(R150Q) mutation affects HsRad51 function, in the present study, we purified the HsRad51(R150Q) mutant. The purified HsRad51(R150Q) was completely proficient in the ATP-hydrolyzing activity. A gel filtration analysis revealed that HsRad51(R150Q) also retained the polymer formation ability. In contrast, the ssDNA- and dsDNA-binding abilities of HsRad51(R150Q) were clearly reduced, as compared to those of HsRad51. These differences in the DNA-binding properties between HsRad51(R150Q) and HsRad51 may be important to account for the tumorigenesis in breast cancer patients with the HsRad51(R150Q) mutation.

• 2007-08-01

著者

• Ishida Takako

  Laboratory Of Structural Biology Graduate School Of Science And Engineering Waseda University

• Sakane Isao

  Institute For Biomedical Engineering Consolidated Research Institute For Advanced Science And Medica

• Kurumizaka Hitoshi

  Laboratory Of Structural Biology Graduate School Of Science And Engineering Waseda University

• Kurumizaka Hitoshi

  Laboratory Of Structural Biology Graduate School Of Science And Engineering Waseda University:instit

• TAKIZAWA Yoshimasa

  Laboratory of Structural Biology, Graduate School of Science and Engineering, Waseda University

• Takizawa Yoshimasa

  Laboratory Of Structural Biology Graduate School Of Science And Engineering Waseda University

• Kurumizaka Hitoshi

  Laboratory Of Cellular & Molecular Biology The Institute Of Physical And Chemical Research (rike

関連論文

• Altered DNA Binding by the Human Rad51-R150Q Mutant Found in Breast Cancer Patients(Biochemistry)
• Homologous Recognition by RecA Protein Using Non-Equivalent Three DNA-Strand-Binding Sites
• In Vivo and in Vitro Footprinting of Nucleosomes and Transcriptional Activators Using an Infrared-Fluorescence DNA Sequencer(Analytical Biochemistry)
• Biochemical analysis of the human ENA/VASP-family proteins, MENA, VASP and EVL, in homologous recombination
• Structure of the CENP-A nucleosome and its implications for centromeric chromatin architecture

スポンサーリンク