Binding of Tau-derived peptide-fused GFP to plant microtubules in Arabidopsis thaliana

PLoS One. 2023 Jun 2;18(6):e0286421. doi: 10.1371/journal.pone.0286421. eCollection 2023.

Abstract

Studies on how exogenous molecules modulate properties of plant microtubules, such as their stability, structure, and dynamics, are important for understanding and modulating microtubule functions in plants. We have developed a Tau-derived peptide (TP) that binds to microtubules and modulates their properties by binding of TP-conjugated molecules in vitro. However, there was no investigation of TPs on microtubules in planta. Here, we generated transgenic Arabidopsis thaliana plants stably expressing TP-fused superfolder GFP (sfGFP-TP) and explored the binding properties and effects of sfGFP-TP on plant microtubules. Our results indicate that the expressed sfGFP-TP binds to the plant microtubules without inhibiting plant growth. A transgenic line strongly expressing sfGFP-TP produced thick fibrous structures that were stable under conditions where microtubules normally depolymerize. This study generates a new tool for analyzing and modulating plant microtubules.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis Proteins* / metabolism
  • Arabidopsis* / metabolism
  • Microtubule-Associated Proteins / metabolism
  • Microtubules / metabolism
  • Peptides / pharmacology

Substances

  • Microtubule-Associated Proteins
  • Arabidopsis Proteins
  • Peptides

Grants and funding

This work was supported by JSPS KAKENHI Grant Numbers JP19K15699 to H.I. from the Japan Society for the Promotion of Science (JSPS), ACT-X (JPMJAX2012 for H.I.), FOREST Program (JPMJFR2034 for H.I.) from the Japan Science and Technology Agency (JST), and JST ERATO (grant number JPMJER1602 for K.N.).