Molecular Architecture of a Kinetochore-microtubule Attachment Site.
From: Department of Biology, University of North Carolina, 607 Fordham hall, CB# 3280, Chapel Hill, NC 27599, USA.
Nature cell biology
- Publish Date: Jun 2006
- ISSN: 1465-7392
- Volume: 8
- Issue: 6
- Pages: 581-5
- Medium: Print
- Language: English
- Citation (JAMA): Joglekar Ajit P, Bouck David C, Molk Jeffrey N, et al. Molecular Architecture of a Kinetochore-microtubule Attachment Site.. Nat. Cell Biol. Jun 2006;8:581-5
Abstract
Kinetochore attachment to spindle microtubule plus-ends is necessary for accurate chromosome segregation during cell division in all eukaryotes. The centromeric DNA of each chromosome is linked to microtubule plus-ends by eight structural-protein complexes. Knowing the copy number of each of these complexes at one kinetochore-microtubule attachment site is necessary to understand the molecular architecture of the complex, and to elucidate the mechanisms underlying kinetochore function. We have counted, with molecular accuracy, the number of structural protein complexes in a single kinetochore-microtubule attachment using quantitative fluorescence microscopy of GFP-tagged kinetochore proteins in the budding yeast Saccharomyces cerevisiae. We find that relative to the two Cse4p molecules in the centromeric histone, the copy number ranges from one or two for inner kinetochore proteins such as Mif2p, to 16 for the DAM-DASH complex at the kinetochore-microtubule interface. These counts allow us to visualize the overall arrangement of a kinetochore-microtubule attachment. As most of the budding yeast kinetochore proteins have homologues in higher eukaryotes, including humans, this molecular arrangement is likely to be replicated in more complex kinetochores that have multiple microtubule attachments.
Mesh Headings (Keywords): Binding Sites, Chromosomal Proteins, Non-Histone, DNA-Binding Proteins, Green Fluorescent Proteins, Kinetochores, Microtubules, Mitotic Spindle Apparatus, Multiprotein Complexes, Saccharomyces cerevisiae Proteins
Check for Full Text / PubMed Unique Identifier (PMID): 16715078
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.