Electron tomography reveals novel microtubule lattice and microtubule organizing centre defects in +TIP mutants

• Published in: PloS one Vol. 8; no. 4; p. e61698
• Main Authors: Höög, Johanna L, Huisman, Stephen M, Brunner, Damian, Antony, Claude
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 16.04.2013; Public Library of Science (PLoS)
• Subjects: Analysis; Baking yeast; Biology; Biophysics; Cell cycle; Defects; Electron Microscope Tomography; Electrons; Homology; Laboratories; Lattices; Life sciences; Microscopy; Microtubule-Associated Proteins - genetics; Microtubule-Associated Proteins - metabolism; Microtubules - metabolism; Molecular biology; Morphology; Mutants; Neoplasm Proteins - genetics; Neoplasm Proteins - metabolism; Physics; Protein families; Proteins; Regulators; Saccharomyces cerevisiae; Schizosaccharomyces - genetics; Schizosaccharomyces - metabolism; Schizosaccharomyces pombe Proteins - genetics; Schizosaccharomyces pombe Proteins - metabolism; Spindle pole bodies; Tips; Tomography; Yeast; Germany
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0061698

Mal3p and Tip1p are the fission yeast (Schizosaccharomyces pombe) homologues of EB1 and CLIP-170, two conserved microtubule plus end tracking proteins (+TIPs). These proteins are crucial regulators of microtubule dynamics. Using electron tomography, we carried out a high-resolution analysis of the phenotypes caused by mal3 and tip1 deletions. We describe the 3-dimensional microtubule organization, quantify microtubule end structures and uncover novel defects of the microtubule lattices. We also reveal unexpected structural modifications of the spindle pole bodies (SPBs), the yeast microtubule organizing centers. In both mutants we observe an increased SPB volume and a reduced number of MT/SPB attachments. The discovered defects alter previous interpretations of the mutant phenotypes and provide new insights into the molecular functions of the two protein families.