A novel ankyrin-repeat protein interacts with the regulatory proteins of inner arm dynein f (I1) of Chlamydomonas reinhardtii.
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.
Ikeda
Kazuho
K
Department of Biological Sciences, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, Japan. kamiyar@biol.s.u-tokyo.ac.jp
Yamamoto
Ryosuke
R
Wirschell
Maureen
M
Yagi
Toshiki
T
Bower
Raqual
R
Porter
Mary E
ME
Sale
Winfield S
WS
Kamiya
Ritsu
R
D000818:Animals; D017089:Ankyrin Repeat; D054468:Axoneme / Q000378:metabolism; D016825:Chlamydomonas reinhardtii / Q000378:metabolism* / Q000502:physiology; D002923:Cilia / Q000378:metabolism; D004398:Dyneins / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D015151:Immunoblotting; D008856:Microscopy, Fluorescence; D009154:Mutation; D011485:Protein Binding; D015800:Protozoan Proteins / Q000235:genetics / Q000378:metabolism*
D015800:Protozoan Proteins; D004398:Dyneins