A novel ankyrin-repeat protein interacts with the regulatory proteins of inner arm dynein f (I1) of Chlamydomonas reinhardtii

Cell Motil Cytoskeleton. 2009 Aug;66(8):448-56. doi: 10.1002/cm.20324.

Abstract

How ciliary and flagellar motility is regulated is a challenging problem. The flagellar movement in Chlamydomonas reinhardtii is in part regulated by phosphorylation of a 138 kD intermediate chain (IC138) of inner arm dynein f (also called I1). In the present study, we found that the axoneme of mutants lacking dynein f lacks a novel protein having ankyrin repeat motifs, registered as FAP120 in the flagellar proteome database. FAP120 is also missing or decreased in the axonemes of bop5, a mutant that has a mutation in the structural gene of IC138 but assembles the dynein f complex. Intriguingly, the amounts of FAP120 in the axonemes of different alleles of bop5 and several dynein f-lacking mutants roughly parallel their contents of IC138. These results suggest a weak but stoichiometric interaction between FAP120 and IC138. We propose that FAP120 functions in the regulatoryprocess as part of a protein complex involving IC138. Cell Motil. Cytoskeleton 2008. (c) 2008 Wiley-Liss, Inc.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Ankyrin Repeat*
  • Axoneme / metabolism
  • Chlamydomonas reinhardtii / metabolism*
  • Chlamydomonas reinhardtii / physiology
  • Cilia / metabolism
  • Dyneins / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Immunoblotting
  • Microscopy, Fluorescence
  • Mutation
  • Protein Binding
  • Protozoan Proteins / genetics
  • Protozoan Proteins / metabolism*

Substances

  • Protozoan Proteins
  • Dyneins