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Eukaryotic Cell, September 2009, p. 1397-1406, Vol. 8, No. 9
1535-9778/09/$08.00+0 doi:10.1128/EC.00378-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.
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and
Jacek Gaertig*
Department of Cellular Biology, University of Georgia, Athens, Georgia 30602
Received 1 December 2008/ Accepted 24 June 2009
In most cilia, the axoneme can be subdivided into three segments: proximal (the transition zone), middle (with outer doublet microtubules), and distal (with singlet extensions of outer doublet microtubules). How the functionally distinct segments of the axoneme are assembled and maintained is not well understood. DYF-1 is a highly conserved ciliary protein containing tetratricopeptide repeats. In Caenorhabditis elegans, DYF-1 is specifically needed for assembly of the distal segment (G. Ou, O. E. Blacque, J. J. Snow, M. R. Leroux, and J. M. Scholey. Nature. 436:583-587, 2005). We show that Tetrahymena cells lacking an ortholog of DYF-1, Dyf1p, can assemble only extremely short axoneme remnants that have structural defects of diverse natures, including the absence of central pair and outer doublet microtubules and incomplete or absent B tubules on the outer microtubules. Thus, in Tetrahymena, DYF-1 is needed for either assembly or stability of the entire axoneme. Our observations support the conserved function for DYF-1 in axoneme assembly or stability but also show that the consequences of loss of DYF-1 for axoneme segments are organism specific.
Published ahead of print on 6 July 2009.
Supplemental material for this article may be found at http://ec.asm.org/.
Present address: Department of Cell Biology, University of Alabama at Birmingham, Birmingham, AL 35294.
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