AI Article Synopsis
- The gamma-tubulin ring complex (gammaTuRC), a protein complex shaped like a lockwasher, is crucial for microtubule nucleation from centrosomes.
- Researchers used a fluorescently-labeled gammaTuRC to track its behavior, finding that it binds to the minus ends of newly formed microtubules.
- The gammaTuRC not only nucleates new microtubules but also acts as a capping protein, preventing further growth and depolymerization at the microtubule's minus ends.
Article Abstract
Microtubule nucleation from centrosomes involves a lockwasher-shaped protein complex containing gamma-tubulin, named the gamma-tubulin ring complex (gammaTuRC). Here we investigate the mechanism by which the gammaTuRC nucleates microtubules, using a direct labelling method to visualize the behaviour of individual gammaTuRCs. A fluorescently-labelled version of the gammaTuRC binds to the minus ends of microtubules nucleated in vitro. Both gammaTuRC-mediated nucleation and binding of the gammaTuRC to preformed microtubules block further minus-end growth and prevent microtubule depolymerization. The gammaTuRC therefore acts as a minus-end-capping protein, as confirmed by electron-microscopic examination of gold-labelled gammaTuRCs. These data support a nucleation model for gammaTuRC function that involves capping of microtubules.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1038/35014051 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Structural insights into the interplay between microtubule polymerases, γ-tubulin complexes and their receptors.
Nat Commun
January 2025
Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), Heidelberg, Germany.
The γ-tubulin ring complex (γ-TuRC) is a structural template for controlled nucleation of microtubules from α/β-tubulin heterodimers. At the cytoplasmic side of the yeast spindle pole body, the CM1-containing receptor protein Spc72 promotes γ-TuRC assembly from seven γ-tubulin small complexes (γ-TuSCs) and recruits the microtubule polymerase Stu2, yet their molecular interplay remains unclear. Here, we determine the cryo-EM structure of the Candida albicans cytoplasmic nucleation unit at 3.
View Article and Find Full Text PDFFirst report of tobacco root rot caused by in Guangdong of China.
Plant Dis
December 2024
Xuchang, China;
Tobacco ( L.) is an economically important crop in China. In April 2024, field tobacco (cv.
View Article and Find Full Text PDFIn situ architecture of a nucleoid-associated biomolecular co-condensate that regulates bacterial cell division.
Proc Natl Acad Sci U S A
January 2025
Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Marburg 35043, Germany.
In most bacteria, cell division depends on the tubulin-homolog FtsZ that polymerizes in a GTP-dependent manner to form the cytokinetic Z-ring at the future division site. Subsequently, the Z-ring recruits, directly or indirectly, all other proteins of the divisome complex that executes cytokinesis. A critical step in this process is the precise positioning of the Z-ring at the future division site.
View Article and Find Full Text PDFStructure of blood cell-specific tubulin and demonstration of dimer spacing compaction in a single protofilament.
J Biol Chem
December 2024
Protein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland, USA. Electronic address:
Microtubule (MT) function plasticity originates from its composition of α- and β-tubulin isotypes and the post-translational modifications of both subunits. Aspects such as MT assembly dynamics, structure, and anticancer drug binding can be modulated by αβ-tubulin heterogeneity. However, the exact molecular mechanism regulating these aspects is only partially understood.
View Article and Find Full Text PDFMolecular architectures of centrosomes in C. elegans embryos visualized by cryo-electron tomography.
Dev Cell
December 2024
Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), 69117 Heidelberg, Germany; Cell Biology and Biophysics Unit, EMBL, 69117 Heidelberg, Germany. Electronic address:
Centrosomes organize microtubules that are essential for mitotic divisions in animal cells. They consist of centrioles surrounded by pericentriolar material (PCM). Questions related to mechanisms of centriole assembly, PCM organization, and spindle microtubule formation remain unanswered, partly due to limited availability of molecular-resolution structural data inside cells.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!