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<p>The ability of bacteria to commit to surface colonization and biofilm formation is a highly regulated process. In this study, we characterized the activity and structure of SadB, initially identified as a key regulator in the transition from reversible to irreversible surface attachment. Our results show that SadB acts as an adaptor protein that tightly regulates the master regulator AmrZ at the post-translational level. SadB directly binds to the C-terminal domain of AmrZ, leading to its rapid degradation, primarily by the Lon protease. Structural analysis suggests that SadB does not directly interact with small molecules upon signal transduction, differing from previous findings in <i>Pseudomonas fluorescens</i>. Instead, the SadB structure supports its role in mediating protein-protein interactions, establishing it as a major checkpoint for biofilm commitment.</p>

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SadB, a mediator of AmrZ proteolysis and biofilm development in Pseudomonas aeruginosa

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年5月13日

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  • Yossi Ben-David,
  • Michael Sporny,
  • Yigal Brochin,
  • Bar Piscon,
  • Shira Roth,
  • Itzhak Zander,
  • Michal Nisani,
  • Sivan Shoshani,
  • Orly Yaron,
  • Sarit Karako-Lampert,
  • Ilana Lebenthal-Loinger,
  • Amos Danielli,
  • Yarden Opatowsky,
  • Ehud Banin

摘要

The ability of bacteria to commit to surface colonization and biofilm formation is a highly regulated process. In this study, we characterized the activity and structure of SadB, initially identified as a key regulator in the transition from reversible to irreversible surface attachment. Our results show that SadB acts as an adaptor protein that tightly regulates the master regulator AmrZ at the post-translational level. SadB directly binds to the C-terminal domain of AmrZ, leading to its rapid degradation, primarily by the Lon protease. Structural analysis suggests that SadB does not directly interact with small molecules upon signal transduction, differing from previous findings in Pseudomonas fluorescens. Instead, the SadB structure supports its role in mediating protein-protein interactions, establishing it as a major checkpoint for biofilm commitment.