ChlamydomonasDIP13 and human NA14: a new class of proteins associated with microtubule structures is involved in cell division

• DOI: 10.1242/jcs.00337
• Publication Date: 2003-03-14T17:08:58Z
• Authors: Frank Pfannenschmid; Verena C. Wimmer; Rosa-Maria Rios; Stefan Geimer; Ulla Kröckel; Andreas Leiherer; Katrin Haller; Yvonne Nemcová; Wolfgang Mages
• Keywords: Male; 0301 basic medicine; Algal Proteins; Molecular Sequence Data; Chromosome Mapping; Nuclear Proteins; Autoantigens; Microtubules; 3. Good health; Mice; Microscopy, Electron; 03 medical and health sciences; Flagella; COS Cells; Chlorocebus aethiops; Animals; Humans; RNA, Antisense; Amino Acid Sequence; Microtubule-Associated Proteins; Cell Division; Chlamydomonas reinhardtii; HeLa Cells

We have cloned and characterized a single copy C. reinhardtii gene containing an open reading frame of 333 nucleotides encoding a 12.7 kDa protein. The novel protein, DIP13, exhibits 60% identity with two mammalian proteins, human NA14 and an unnamed mouse protein. Homologous sequences are also present in several protozoan, trematode and fish genomes, but no homologs have been found in the completed genomes of yeast, Drosophila, C. elegans and A. thaliana. By using a specific antibody we have localized DIP13 to microtubule structures, namely basal bodies, flagellar axonemes and cytoplasmic microtubules. Anti-DIP13 antibody also specifically recognized human NA14 by immunofluorescence and stained basal bodies and flagella of human sperm cells as well as the centrosome of HeLa cells. Expression of the DIP13 open reading frame in antisense orientation in Chlamydomonas resulted in multinucleate, multiflagellate cells,which suggests a role for this protein in ensuring proper cell division. Thus,DIP13/NA14 could represent the founding members of a new class of highly conserved proteins that are associated with microtubule structures.