Open AccessA novel ankyrin‐repeat protein interacts with the regulatory proteins of inner arm dynein f (I1) of Chlamydomonas reinhardtii
Author(s) -
Ikeda Kazuho,
Yamamoto Ryosuke,
Wirschell Maureen,
Yagi Toshiki,
Bower Raqual,
Porter Mary E.,
Sale Winfield S.,
Kamiya Ritsu
Publication year - 2009
Publication title -
cell motility and the cytoskeleton
Language(s) - English
Resource type - Journals
eISSN - 1097-0169
pISSN - 0886-1544
DOI - 10.1002/cm.20324
Subject(s) - dynein , biology , axoneme , chlamydomonas reinhardtii , chlamydomonas , microbiology and biotechnology , microtubule , mutant , ankyrin repeat , flagellum , cilium , dynactin , cytoskeleton , genetics , gene , cell
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. © 2008 Wiley‐Liss, Inc.