Authors:

Mateus Rocha Ripari

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About Paper:

Ralstonia solanacearum (Rs), a significant bacterial plant pathogen affecting crops worldwide, deploys type III effector (T3E) proteins, such as RipU, to promote colonization and disease development. This effort aims to study the core effector protein RipU from Rs strain K60 to understand the domains responsible for its interactions and localization within plant cells. Previously, RipUK60 was found to co-localize with microtubules and disrupted microtubule organization in transient expression assays. In the current study, truncated versions of RipU K60 fused to fluorescent proteins were cloned and expressed in Nicotiana benthamiana leaf tissue using Agrobacterium tumefaciens-mediated transient expression. Confocal microscopy was used to analyze protein localization and colocalization with cytoskeleton markers and yeast two- hybrid assays evaluated direct interactions between the T3E protein, actin, and tubulin. RipU K60 was found to associate with both actin and tubulin, disrupting cytoskeleton organization. By investigating truncated versions and their interaction with cytoskeletal proteins, the study proposes domains responsible for the distinct localizations and interactions. This provides valuable insights into RipU functionality, post- translational modification, and potential targets for future breeding programs. Keywords: Ralstonia; RipU; Effector; Cytoskeleton; T3E

Source:

Purdue University / 2025

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Co-authors:

Mateus Rocha Ripari