AI Article Synopsis
- The SulA protein in E. coli and similar bacteria inhibits cell division by blocking Z-ring formation through its interaction with FtsZ, though the exact mechanism isn't fully clear.
- Previous studies on Pseudomonas aeruginosa SulA showed it could dimerize using X-ray crystallography but didn't confirm this in living cells.
- This paper utilizes a bacterial two-hybrid system to confirm that both P. aeruginosa and E. coli SulA proteins can dimerize.
Article Abstract
The SulA protein of Escherichia coli and related bacteria interacts directly with FtsZ, blocking cell division by disrupting Z-ring formation, yet the precise mechanism remains not fully understood. Previous demonstrations of Pseudomonas aeruginosa SulA's dimerization capability were confined to X-ray crystallography and lacked confirmation under in vivo conditions. Additionally, uncertainty persisted regarding the dimerization potential of E. coli's SulA protein. This paper employs a bacterial two-hybrid system to establish that both P. aeruginosa and E. coli SulA proteins indeed possess the capacity for dimerization.
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| http://dx.doi.org/10.1016/j.abb.2023.109826 | DOI Listing |
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