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First published online August 17, 2004

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Fuel supply for flagella

Cilia and flagella have a characteristic 9 + 2 structure in which a ring of nine microtubule doublets surrounds a central pair of two microtubules and numerous associated proteins. The central pair is critical for motility, but we know little about its associated proteins and their functions. On p. 4179, Hui Zhang and David Mitchell reveal that one of these, Cpc1, is responsible for refuelling the organelle. Chlamydomonas cpc1 mutants exhibit reduced flagellar beating. The authors have cloned the Cpc1 gene and use an anti-Cpc1 antibody to show that it encodes a conserved component of a 16S complex associated with the central pair. Sequence analysis indicates that Cpc1 has an unusual adenylate kinase domain. Since adenylate kinases generate ATP from ADP, Zhang and Mitchell examined the effect of increasing the concentration of ATP on flagellar beating in cpc1 mutants: significantly, the increase suppresses the beating defect. The authors conclude that, under normal conditions, Cpc1 is needed to maintain normal levels of flagellar ATP - if ATP concentrations are high, it is no longer necessary.

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Related articles in JCS:

Cpc1, a Chlamydomonas central pair protein with an adenylate kinase domain

Hui Zhang and David R. Mitchell
JCS 2004 117: 4179-4188. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?