The Chlamydomonas PF6 locus encodes a large alanine/proline-rich polypeptide that is required for assembly of a central pair projection and regulates flagellar motility

被引:71
作者
Rupp, G
O'Toole, E
Porter, ME [1 ]
机构
[1] Univ Minnesota, Sch Med, Dept Genet, Minneapolis, MN 55455 USA
[2] Univ Minnesota, Sch Med, Dept Cell Biol, Minneapolis, MN 55455 USA
[3] Univ Minnesota, Sch Med, Dept Dev, Minneapolis, MN 55455 USA
[4] Univ Colorado, Dept Mol Cellular & Dev Biol, Boulder, CO 80309 USA
关键词
D O I
10.1091/mbc.12.3.739
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Efficient motility of the eukaryotic flagellum requires precise temporal and spatial control of its constituent dynein motors. The central pair and its associated structures have been implicated as important members of a signal transduction cascade that ultimately regulates dynein arm activity. To identify central pair components involved in this process, we characterized a Chlamydomonas motility mutant (pf6-2) obtained by insertional mutagenesis. pf6-2 flagella twitch ineffectively and lack the 1a projection on the C1 microtubule of the central pair. Transformation with constructs containing a full-length, wild-type copy of the PF6 gene rescues the functional, structural, and biochemical defects associated with the pf6 mutation. Sequence analysis indicates that the PF6 gene encodes a large polypeptide that contains numerous alanine-rich, proline-rich, and basic domains and has limited homology to an expressed sequence tag derived from a human testis cDNA library. Biochemical analysis of an epitope-tagged PF6 construct demonstrates that the PF6 polypeptide is an axonemal component that cosediments at 12.6S with several other polypeptides. The PF6 protein appears to be an essential component required for assembly of some of these polypeptides into the Cl-1a projection.
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页码:739 / 751
页数:13
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