Author(s): Jana, Swadhin C ; Machado, Pedro ; Bettencourt-Dias, Mónica
Date: 2012
Persistent ID: http://hdl.handle.net/10400.7/834
Origin: ARCA - Access to Research and Communication Annals
Project/scholarship: info:eu-repo/grantAgreement/FCT/3599-PPCDT/105602/PT ; info:eu-repo/grantAgreement/EC/FP7/261344/EU;
Subject(s): Animals; Cilia; Microtubules; Basal Body
The deposited article is a post-print version and has been submitted to peer review.
This publication hasn't any creative commons license associated.
There is no public supplementary material available.
The Basal Body (BB) acts as the template for the axoneme, the microtubule‐basedstructure of cilia and flagella. Although several proteins were recently implicatedin both centriole and BB assembly and function, their molecular mechanisms are stillpoorly characterized. In this issue of The EMBO journal, Li and coworkersdescribe for the first time the near‐native structure of the BB at 33 Åresolution obtained by Cryo‐Electron Microscopy analysis of wild‐type (WT) isolatedChlamydomonas BBs. They identified several uncharacterized non‐tubulinstructures and variations along the length of the BB, which likely reflect thebinding and function of numerous macromolecular complexes. These complexes areexpected to define BB intrinsic properties, such as its characteristic structure andstability. Similarly to the high‐resolution structures of ribosome and nuclear porecomplexes, this study will undoubtedly contribute towards the future analysis ofcentriole and BB biogenesis, maintenance and function.
Fundação para a Ciência e Tecnologia grant: (PTDC/BIA‐BCM/105602/2008); EMBO Installation Grant; Instituto Gulbenkian de Ciência; ERC grant(261344—CentriolStructNumber).
