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University of Massachusetts Medical School Faculty Publications

2014

Amino Acid Sequence; Axoneme; Chlamydomonas reinhardtii; Conserved Sequence; Cytoplasm; Enzyme Stability; Flagella; Peptide Synthases; Plant Proteins; Protein Binding; Protein Processing, Post-Translational; Protein Transport; Sequence Homology, Amino Acid; Tubulin

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Full-Text Articles in Molecular Biology

A Conserved Flagella-Associated Protein In Chlamydomonas, Fap234, Is Essential For Axonemal Localization Of Tubulin Polyglutamylase Ttll9, Tomohiro Kubo, Haru-Aki Yanagisawa, Zhongmei Liu, Rie Shibuya, Masafumi Hirono, Ritsu Kamiya Jan 2014

A Conserved Flagella-Associated Protein In Chlamydomonas, Fap234, Is Essential For Axonemal Localization Of Tubulin Polyglutamylase Ttll9, Tomohiro Kubo, Haru-Aki Yanagisawa, Zhongmei Liu, Rie Shibuya, Masafumi Hirono, Ritsu Kamiya

University of Massachusetts Medical School Faculty Publications

Tubulin undergoes various posttranslational modifications, including polyglutamylation, which is catalyzed by enzymes belonging to the tubulin tyrosine ligase-like protein (TTLL) family. A previously isolated Chlamydomonas reinhardtii mutant, tpg1, carries a mutation in a gene encoding a homologue of mammalian TTLL9 and displays lowered motility because of decreased polyglutamylation of axonemal tubulin. Here we identify a novel tpg1-like mutant, tpg2, which carries a mutation in the gene encoding FAP234, a flagella-associated protein of unknown function. Immunoprecipitation and sucrose density gradient centrifugation experiments show that FAP234 and TTLL9 form a complex. The mutant tpg1 retains FAP234 in the cell body and flagellar ...