Evaluating the microtubule cytoskeleton and its interacting proteins in monocots by mining the rice genome

Ann Bot. 2009 Feb;103(3):387-402. doi: 10.1093/aob/mcn248. Epub 2008 Dec 23.

Abstract

Background: Microtubules (MTs) are assembled by heterodimers of alpha- and beta-tubulins, which provide tracks for directional transport and frameworks for the spindle apparatus and the phragmoplast. MT nucleation and dynamics are regulated by components such as the gamma-tubulin complex which are conserved among eukaryotes, and other components which are unique to plants. Following remarkable progress made in the model plant Arabidopsis thaliana toward revealing key components regulating MT activities, the completed rice (Oryza sativa) genome has prompted a survey of the MT cytoskeleton in this important crop as a model for monocots.

Scope: The rice genome contains three alpha-tubulin genes, eight beta-tubulin genes and a single gamma-tubulin gene. A functional gamma-tubulin ring complex is expected to form in rice as genes encoding all components of the complex are present. Among proteins that interact with MTs, compared with A. thaliana, rice has more genes encoding some members such as the MAP65/Ase1p/PRC1 family, but fewer for the motor kinesins, the end-binding protein EB1 and the mitotic kinase Aurora. Although most known MT-interacting factors have apparent orthologues in rice, no orthologues of arabidopsis RIC1 and MAP18 have been identified in rice. Among all proteins surveyed here, only a few have had their functions characterized by genetic means in rice. Elucidating functions of proteins of the rice MT cytoskeleton, aided by recent technical advances made in this model monocot, will greatly advance our knowledge of how monocots employ their MTs to regulate their growth and form.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Genome, Plant / genetics*
  • Microtubules / metabolism*
  • Oryza / enzymology
  • Oryza / genetics*
  • Plant Proteins / metabolism*
  • Protein Binding
  • Species Specificity

Substances

  • Plant Proteins