Format

Send to

Choose Destination
PLoS Genet. 2017 Sep 11;13(9):e1006996. doi: 10.1371/journal.pgen.1006996. eCollection 2017 Sep.

Chlamydomonas DYX1C1/PF23 is essential for axonemal assembly and proper morphology of inner dynein arms.

Author information

1
Department of Biological Sciences, Graduate School of Science, Osaka University, Osaka, Japan.
2
Laboratory of Biomolecular Research, Paul Scherrer Institute, Villigen PSI, Switzerland.
3
Department of Biology, Oglethorpe University, Atlanta, Georgia, United States of America.
4
Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo, Japan.
5
Department of Cell Biology, Emory University School of Medicine, Atlanta, Georgia, United States of America.
6
Shimoda Marine Research Center, University of Tsukuba, Shizuoka, Japan.
7
Department of Genetics, Washington University School of Medicine, St. Louis, Missouri, United States of America.
8
Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, Connecticut, United States of America.

Abstract

Cytoplasmic assembly of ciliary dyneins, a process known as preassembly, requires numerous non-dynein proteins, but the identities and functions of these proteins are not fully elucidated. Here, we show that the classical Chlamydomonas motility mutant pf23 is defective in the Chlamydomonas homolog of DYX1C1. The pf23 mutant has a 494 bp deletion in the DYX1C1 gene and expresses a shorter DYX1C1 protein in the cytoplasm. Structural analyses, using cryo-ET, reveal that pf23 axonemes lack most of the inner dynein arms. Spectral counting confirms that DYX1C1 is essential for the assembly of the majority of ciliary inner dynein arms (IDA) as well as a fraction of the outer dynein arms (ODA). A C-terminal truncation of DYX1C1 shows a reduction in a subset of these ciliary IDAs. Sucrose gradients of cytoplasmic extracts show that preassembled ciliary dyneins are reduced compared to wild-type, which suggests an important role in dynein complex stability. The role of PF23/DYX1C1 remains unknown, but we suggest that DYX1C1 could provide a scaffold for macromolecular assembly.

PMID:
28892495
PMCID:
PMC5608425
DOI:
10.1371/journal.pgen.1006996
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Public Library of Science Icon for PubMed Central
Loading ...
Support Center