Yung-Chih Chen
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chenyc1101.bsky.social
Yung-Chih Chen
@chenyc1101.bsky.social
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B.S. in Life Sciences @ NUK |
Research assistant @ IBC, Academia Sinica |
Interested in Microbiology, Structural Biology, Computational Biology
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Reposted by Yung-Chih Chen
plosbiology.org
Bacteria use toxic effectors to outcompete other bacteria. @seeyeunting.bsky.social &co show that the cysteine protease Cpe1, a widespread #toxin in Gram negative #bacteria, inhibits replication in competitors by cleaving & disabling DNA #topoisomerases GyrB & ParE @plosbiology.org 🧪 plos.io/4dyEVXL
Top: Ribbon diagrams of E. coli GyrB (left) and ParE (right) before and after cleavage by Cpe1tox. Crystal structures of the 43-kDa ATPase domain of E. coli GyrB (PDB: 4PRV) and ParE (PDB: 1S16) were used. Residues of the consensus sequence (LHAGGKF) are shown in yellow. Structure related to the small fragments after Cpe1tox cleavage are indicated as pink ribbons. Predicted structures after cleavage at the double glycine motif demonstrated disruption of the ATPase domain of both GyrB and ParE. Bottom: Working model of how Cpe1 intoxicates bacteria. During interbacterial competition, Cpe1 targets and cleaves the ATPase domains of GyrB and ParE in target cells. The cleavage leads to accumulations of unrelaxed supercoils and precatenanes, disrupts DNA segregation, and ultimately inhibits cell division and growth. In the Cpe1-producing cells or kin cells expressing the immunity protein Cpi1, Cpe1 toxicity is neutralized through direct interaction between Cpe1 and Cpi1.
May 28, 2025 at 5:30 PM