JCB logo
Accuri Cytometers
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

Published online 1 June 2004. doi:10.1083/jcb1655iti5
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 165, Number 5, 603-603
This Article
Right arrow PDF (Full Text)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sreenivasan, A.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Sreenivasan, A.
Related Collections
Right arrowRelated Article
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

In This Issue

Building centrioles


Bld10p (gold particles) localizes to the proximal part of the basal body (bb).

Centrioles and surrounding centrosomal material nucleate both mitotic spindles and interphase microtubule asters, but centrioles are not an easy structure to dissect with either biochemistry or genetics. There are budding yeast mutants that arrest at various stages of maturation of the spindle pole body (SPB), but the SPB and mammalian centriole bear no physical resemblance to each other despite sharing some proteins and fulfilling the same function.

Matsuura et al. (page 663) therefore resort to a trick of Chlamydomonas biology. In this unicellular green algae, the basal body has its normal function of nucleating flagellar microtubules during interphase, but it also switches to act as a centriole during cell division. This dual role gives the authors an easily identifiable phenotype for the isolation of mutants defective in centriole function.

Using insertional mutagenesis, the team isolated 74 Chlamydamonas mutants lacking flagella. Most of the mutants lack flagellum-specific proteins, but one mutant, bld10, which grew very slowly and exhibited abnormal cell division, piqued their interest. Upon closer examination, they found that bld10 mutants had no basal bodies. Before this discovery, it was not known if the complete elimination of basal bodies would result in death. These findings suggest that insertional mutagenesis could be used to find and characterize the more than 200 other potential players involved in basal body assembly.

Immunogold labeling showed that Bld10p localizes to the cartwheel, a complex circular structure where microtubules originate. The authors speculate that Bld10p's localization means that the cartwheel plays a critical part in putting together basal bodies. {blacksquare}



Aparna Sreenivasan

aparnas{at}nasw.org


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?

Related Article

Bld10p, a novel protein essential for basal body assembly in Chlamydomonas: localization to the cartwheel, the first ninefold symmetrical structure appearing during assembly
Kumi Matsuura, Paul A. Lefebvre, Ritsu Kamiya, and Masafumi Hirono
J. Cell Biol. 2004 165: 663-671. [Abstract] [Full Text] [PDF]




This Article
Right arrow PDF (Full Text)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sreenivasan, A.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Sreenivasan, A.
Related Collections
Right arrowRelated Article
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?


  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents