Abstract
Mutations at CPC1 disrupt assembly of a central pair microtubule-associated complex and alter flagellar beat frequency in Chlamydomonas. Sequences of wild-type genomic clones that complement cpc1, and of corresponding cDNAs, reveal the gene product to be a 205 kDa protein with two predicted functional domains, a single EF hand motif near the C-terminus and an unusual centrally located adenylate kinase domain. Homologs are expressed in mammals (testis and tracheal cilia) as well as ciliated lower eukaryotes. Western blots confirm that Cpc1 is one of six subunits in a 16S central pair-associated complex. Motility defects associated with cpc1 alleles in vivo are partially rescued in vitro by reactivation of axonemes or cell models in saturating concentrations of ATP; thus the Cpc1 complex is essential for maintaining normal ATP concentrations in the flagellum.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Triphosphate / metabolism
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Adenylate Kinase / chemistry
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Adenylate Kinase / genetics*
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Adenylate Kinase / metabolism
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Amino Acid Sequence
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Animals
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Base Sequence
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Chlamydomonas reinhardtii / enzymology
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Chlamydomonas reinhardtii / genetics*
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Chlamydomonas reinhardtii / ultrastructure
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Cloning, Molecular
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DNA, Complementary / analysis
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DNA, Complementary / genetics
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Flagella / enzymology*
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Flagella / ultrastructure
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Macromolecular Substances
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Microtubule-Associated Proteins / chemistry
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Microtubule-Associated Proteins / genetics
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Microtubule-Associated Proteins / metabolism
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Microtubules / metabolism
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Microtubules / ultrastructure
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Molecular Sequence Data
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Protein Structure, Tertiary / genetics
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Protozoan Proteins / chemistry
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Protozoan Proteins / genetics*
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Protozoan Proteins / metabolism
Substances
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DNA, Complementary
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Macromolecular Substances
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Microtubule-Associated Proteins
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Protozoan Proteins
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Adenosine Triphosphate
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Adenylate Kinase