Yajie Gu

2 months ago | cell.com | Yajie Gu |Huan Li |Amar Deep |Eray Enustun |Dapeng Zhang |Kevin Corbett

Keywords anti-phage immunity DUF4263 PD-(D/E)XK nuclease Whirly domain two-component signalling Introduction The ongoing evolutionary conflict between bacteria and their viral pathogens (bacteriophages or phages) has driven the development of myriad bacterial immune systems that fight infection and an equally complex array of viral factors that counter these systems.1,2 The most well-understood bacterial immune systems, restriction-modification systems and CRISPR-Cas systems, are found in a...

Nov 21, 2024 | biorxiv.org | Minheng Gong |Qiaozhen Ye |Yajie Gu |Lydia R Chambers

AbstractBacteria possess a variety of operons with homology to eukaryotic ubiquitination pathways that encode predicted E1, E2, E3, deubiquitinase, and ubiquitin-like proteins. Some of these pathways have recently been shown to function in anti-bacteriophage immunity, but the biological functions of others remain unknown.

Sep 27, 2024 | biorxiv.org | Spencer Gordon |Alyssa Rodriguez |Yajie Gu |Kevin Corbett

AbstractDuring meiosis, the parental chromosomes are drawn together to enable exchange of genetic information. Chromosomes are aligned through the assembly of a conserved interface, the synaptonemal complex, composed of a central region that forms between two parallel chromosomal backbones called axes. Here we identify the axis-central region interface in C. elegans, containing a conserved positive patch on the axis component HIM-3 and the C-terminus of the central region protein SYP-5.

Nov 3, 2023 | mdpi.com | Ling Pei |Hong Zhou |Wenxin Du |Yajie Gu

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Aug 10, 2023 | biorxiv.org | Yajie Gu |Huan Li |Amar Deep |Eray Enustun

AbstractProkaryotes encode diverse anti-bacteriophage immune systems, including the single-protein Shedu nuclease. Here we reveal the structural basis for activation of Bacillus cereus Shedu. In the inactive homotetramer, a key catalytic residue in Shedu's nuclease domain is sequestered away from the catalytic site. Activation involves a conformational change that completes the active site and promotes assembly of a homo-octamer for coordinated double-strand DNA cleavage.