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Homologues of radial spoke head proteins interact with Ca2+/calmodulin in Tetrahymena cilia
- Source :
- Journal of biochemistry. 140(4)
- Publication Year :
- 2006
-
Abstract
- Calmodulin (CaM) is an axonemal component. To examine the pathway of Ca(2+)/CaM signaling in cilia, using Ca(2+)/CaM-affinity column, we identified seven Ca(2+)/CaM-associated proteins from a crude dynein fraction and isolated 62 kDa (p62) and 66 kDa (p66) Ca(2+)/CaM-associated proteins in Tetrahymena cilia. The amino acid sequences deduced from the p62 and p66 cDNA sequences suggested that these proteins were similar to Chlamydomonas radial spoke proteins 4 and 6 (RSP4 and RSP6), components of the radial spoke head, and sea urchin sperm p63, which is a homologue of RSP4/6, and isolated as a key component that affect flagellar bending patterns. Although p62 and p66 do not have a conventional CaM-binding site, those have consecutive sequences which showed high normalized scores (>or= 5) from a CaM target database. These consecutive sequences were also found in RSP4, RSP6, and p63. These radial spoke heads proteins have a high similarity region composed of 15 amino acids between the five proteins. Immunoelectron microscopy using anti-CaM antibody showed that CaM was localized along the outer edge of the curved central pair microtubules in axoneme. Therefore, it is possible that the interaction between Ca(2+)/CaM and radial spoke head control axonemal curvature in the ciliary and flagellar waveform.
- Subjects :
- Axoneme
Male
animal structures
Calmodulin
Immunoelectron microscopy
Dynein
Molecular Sequence Data
Protozoan Proteins
Biochemistry
Microtubules
Protein structure
Microscopy, Electron, Transmission
Microtubule
Animals
Amino Acid Sequence
Cilia
Molecular Biology
Plant Proteins
biology
Sequence Homology, Amino Acid
Radial spoke head
Tetrahymena
Dyneins
General Medicine
biology.organism_classification
Cell biology
Protein Structure, Tertiary
biology.protein
Calcium
Protein Binding
Signal Transduction
Subjects
Details
- ISSN :
- 0021924X
- Volume :
- 140
- Issue :
- 4
- Database :
- OpenAIRE
- Journal :
- Journal of biochemistry
- Accession number :
- edsair.doi.dedup.....d68815c42101dcf9d9ba07d59ce70e8e