scholarly journals OsRAD17 Is Required for Meiotic Double-Strand Break Repair and Plays a Redundant Role With OsZIP4 in Synaptonemal Complex Assembly

2018 ◽  
Vol 9 ◽  
Author(s):  
Qing Hu ◽  
Chao Zhang ◽  
Zhihui Xue ◽  
Lijun Ma ◽  
Wei Liu ◽  
...  
2018 ◽  
Vol 1 (3) ◽  
pp. e201800021
Author(s):  
Noriko Hosoya ◽  
Masato Ono ◽  
Kiyoshi Miyagawa

The synaptonemal complex is a proteinaceous structure essential for meiotic recombination, and its components have been assumed to play a role exclusively in the germ line. However, SYCE2, a component constituting the synaptonemal complex, is expressed at varying levels in somatic cells. Considering its potent protein-binding activities, it may be possible that SYCE2 plays a somatic role by affecting nuclear functions. Here, we show that SYCE2 constitutively insulates HP1α from trimethylated histone H3 lysine 9 (H3K9me3) to promote DNA double-strand break repair. Unlike other HP1α-binding proteins, which use the canonical PXVXL motifs for their bindings, SYCE2 interacts with the chromoshadow domain of HP1α through its N-terminal hydrophobic sequence. SYCE2 reduces HP1α-H3K9me3 binding without affecting H3K9me3 levels and potentiates ataxia telangiectasia mutated–mediated double-strand break repair activity even in the absence of exogenous DNA damage. Such a somatic role of SYCE2 is ubiquitously observed even if its expression levels are low. These findings suggest that SYCE2 plays a somatic role in the link between the nuclear microenvironment and the DNA damage response potentials as a scaffold of HP1α localization.


1997 ◽  
Vol 2 (8) ◽  
pp. 487-498 ◽  
Author(s):  
Drora Zenvirth ◽  
Josef Loidl ◽  
Shoshana Klein ◽  
Ayelet Arbel ◽  
Ronen Shemesh ◽  
...  

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