Domain Structure of the Redβ Single-Strand Annealing Protein: the C-terminal Domain is Required for Fine-Tuning DNA-binding Properties, Interaction with the Exonuclease Partner, and Recombination in vivo
详细信息 查看全文
- 作者：Christopher E. Smith1 ; 2 ; Charles E. Bell1 ; 2 ; 3 ; bell.489@osu.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：ssDNA ; single-stranded DNA ; dsDNA ; double-stranded DNA ; λexo ; λ exonuclease ; HR ; homologous recombination ; NHEJ ; non-homologous end joining ; SSA ; single strand annealing ; FP ; fluorescence polarization ; BAC ; bacterial artificial chromosome ; EM ; electron microscopy ; AFM ; atomic force microscopy ; CD ; circular dichroism
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：13 February 2016
- 年：2016
- 卷：428
- 期：3
- 页码：561-578
- 全文大小：1412 K
文摘
- •
Redβ is a 261 amino acid protein from bacteriophage λ that promotes single strand annealing by mechanism that is not well understood.
- •
Residues 1–177 of Redβ contain the determinants for DNA binding and self-oligomerization.
- •
Residues 182–261 of Redβ contain the determinants for binding to λ exonuclease.
- •
Removal of the last eleven amino acids from the C-terminus of Redβ disrupts the complex with λ exonuclease and dsDNA and ssDNA recombination in vivo.
© 2004-2018 中国地质图书馆版权所有 京ICP备05064691号 京公网安备11010802017129号 地址：北京市海淀区学院路29号 邮编：100083 电话：办公室：(+86 10)66554848；文献借阅、咨询服务、科技查新：66554700 |