OsFH3 Encodes a Type II Formin Required for Rice Morphogenesis

Int J Mol Sci. 2021 Dec 9;22(24):13250. doi: 10.3390/ijms222413250.

Abstract

The actin cytoskeleton is crucial for plant morphogenesis, and organization of actin filaments (AF) is dynamically regulated by actin-binding proteins. However, the roles of actin-binding proteins, particularly type II formins, in this process remain poorly understood in plants. Here, we report that a type II formin in rice, Oryza sativa formin homolog 3 (OsFH3), acts as a major player to modulate AF dynamics and contributes to rice morphogenesis. osfh3 mutants were semi-dwarf with reduced size of seeds and unchanged responses to light or gravity compared with mutants of osfh5, another type II formin in rice. osfh3 osfh5 mutants were dwarf with more severe developmental defectiveness. Recombinant OsFH3 could nucleate actin, promote AF bundling, and cap the barbed end of AF to prevent elongation and depolymerization, but in the absence of profilin, OsFH3 could inhibit AF elongation. Different from other reported type II formins, OsFH3 could bind, but not bundle, microtubules directly. Furthermore, its N-terminal phosphatase and tensin homolog domain played a key role in modulating OsFH3 localization at intersections of AF and punctate structures of microtubules, which differed from other reported plant formins. Our results, thus, provide insights into the biological function of type II formins in modulating plant morphology by acting on AF dynamics.

Keywords: OsFH3; localization; morphological defects; profilin–actin complex; rice.

MeSH terms

  • Actin Cytoskeleton / metabolism
  • Formins / chemistry
  • Formins / genetics*
  • Formins / metabolism*
  • Morphogenesis
  • Mutation
  • Organ Size
  • Oryza / genetics
  • Oryza / growth & development*
  • Oryza / metabolism
  • Plant Proteins / chemistry
  • Plant Proteins / genetics
  • Plant Proteins / metabolism
  • Protein Domains
  • Seeds / genetics
  • Seeds / growth & development
  • Seeds / metabolism

Substances

  • Formins
  • Plant Proteins