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Published on: July 8, 2014
Regulatory role of nucleotides in axonemal function
S Kinoshita1, T Miki-Noumura, C K Omoto
1Department of Biology, Ochanomizu University, Tokyo, Japan.
Cell Motility and the Cytoskeleton
|January 1, 1995
Summary
High ATP concentrations inhibit axonemal sliding disintegration, but ADP relieves this effect. Nucleotide binding to regulatory sites controls sliding extent for effective ciliary and flagellar bending.
Area of Science:
- Biochemistry
- Cell Biology
- Biophysics
Background:
- Axonemal sliding is crucial for ciliary and flagellar motility.
- The extent of doublet sliding, not just velocity, is critical for effective axonemal bending.
- Understanding nucleotide regulation of sliding extent is key to comprehending motility mechanisms.
Purpose of the Study:
- To investigate the effects of ATP, ADP, and ATP analogs on the extent of axonemal sliding disintegration.
- To elucidate the regulatory role of nucleotides in controlling sliding extent.
- To propose a model for nucleotide-mediated regulation of axonemal function.
Main Methods:
- Utilized the turbidimetric assay to measure sliding disintegration of Tetrahymena axonemes.
- Examined the impact of varying concentrations of ATP, ADP, and ribose-modified ATP analogs (anthraniloylATP, methylanthraniloylATP) on sliding extent.
Main Results:
- ATP is necessary for sliding disintegration, but high concentrations inhibit the extent.
- ADP addition relieved the inhibition caused by high ATP concentrations.
- Ribose-modified ATP analogs showed concentration-dependent sliding disintegration without inhibition at higher concentrations.
Conclusions:
- High ATP concentration inhibits the extent of sliding disintegration, with ADP acting as a relief factor.
- A model is proposed where nucleotide binding to regulatory sites modulates the affinity of cooperative active sites.
- This mechanism explains how nucleotides regulate the sliding extent essential for effective axonemal bending.
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