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Structure of 5-hydroxymethylcytosine-specific restriction enzyme, AbaSI, in complex with DNA by John R. Horton; Janine G. Borgaro; Rose M. Griggs; Aine Quimby; Shengxi Guan; Xing Zhang; Geoffrey G. Wilson; Yu Zheng; Zhenyu Zhu; Xiaodong Cheng is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
What is Structure of 5-hydroxymethylcytosine-specific restriction enzyme, AbaSI, in complex with DNA about?
AbaSI, a member of the PvuRts1I-family of modification-dependent restriction endonucleases, cleaves deoxyribonucleic acid (DNA) containing 5-hydroxymethylctosine (5hmC) and glucosylated 5hmC (g5hmC), but not DNA containing unmodified cytosine. AbaSI has been used as a tool for mapping the genomic locations of 5hmC, an important epigenetic modification in the DNA of higher organisms. Here we report the crystal structures of AbaSI in the presence and absence of DNA. These structures provide considerable, although incomplete, insight into how this enzyme acts. AbaSI appears to be mainly a homodimer in solution, but interacts with DNA in our structures as a homotetramer. Each AbaSI subunit comprises an N-terminal, Vsr-like, cleavage domain containing a single catalytic site, and a C-terminal, SRA-like, 5hmC-binding domain. Two N-terminal helices mediate most of the homodimer interface. Dimerization brings together the two catalytic sites required for double-strand cleavage, and separates the 5hmC binding-domains by ∼70 Å, consistent with the known activity of AbaSI which cleaves DNA optimally between symmetrically modified cytosines ∼22 bp apart. The eukaryotic SET and RING-associated
Who reads Structure of 5-hydroxymethylcytosine-specific restriction enzyme, AbaSI, in complex with DNA?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- John R. Horton; Janine G. Borgaro; Rose M. Griggs; Aine Quimby; Shengxi Guan; Xing Zhang; Geoffrey G. Wilson; Yu Zheng; Zhenyu Zhu; Xiaodong Cheng
- Publisher
- Oxford University Press; London: Information Retrieval; Oxford: Oxford University Press; Oxford University Press (OUP) (ISSN 0305-1048)
- Published
- 2014
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)