This is the C-terminal domain found in GEN1 resolvase. It is composed of three-strand antiparallel beta sheets and four alpha helices [1]. GEN1 protein, a member of the XPG/Rad2 family of structure-selective endonucleases, is specialized for the cleavage of Holliday junction recombination intermediates [2]. Structural comparison indicates that the C-terminal domain is similar to a series of chromobox homology proteins [1]. Functional analysis indicates that the chromodomain provides an additional DNA binding site necessary for efficient HJ cleavage, and its truncation severely hampers GEN1's catalytic activity [3]. [1]. 26686639. Crystal Structure of a Eukaryotic GEN1 Resolving Enzyme Bound to. DNA.. Liu Y, Freeman AD, Declais AC, Wilson TJ, Gartner A, Lilley DM;. Cell Rep. 2015;13:2565-2575.. [2]. 28049850. Resolution of single and double Holliday junction recombination. intermediates by GEN1.. Shah Punatar R, Martin MJ, Wyatt HD, Chan YW, West SC;. Proc Natl Acad Sci U S A. 2017;114:443-450.. [3]. 26682650. Human Holliday junction resolvase GEN1 uses a chromodomain for. efficient DNA recognition and cleavage.. Lee SH, Princz LN, Klugel MF, Habermann B, Pfander B,. Biertumpfel C;. Elife. 2015; [Epub ahead of print] (from Pfam)
- Date:
- 2024-08-14