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

This Article Full Text (PDF, 208K) PPT slides of all figures Alert me when this article is cited Services Email this article Similar articles in this journal Alert me to new content in the JCB Download to citation manager Citing Articles Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Dove, A. W. Search for Related Content PubMed Articles by Dove, A. W. Related Collections Related Article Social Bookmarking                            What's this?

© The Rockefeller University Press, 0021-9525/2002/8/383-a $5.00
The Journal of Cell Biology, Volume 158, Number 3, August 5, 2002 383-a-383

BAF goes nuclear

BAF bridges DNA (binding at either end) and nuclear envelope proteins (binding in the middle).

Barrier-to-autointegration factor (BAF) was first described as a cellular activity that prevents retroviral DNA from undergoing suicidal autointegration, but its function in uninfected cells remained obscure. Segura-Totten et al. (page 475) have now performed a detailed biochemical characterization of BAF. The work defines critical functional motifs of this DNA-bridging protein, and suggests that BAF is essential for chromatin decondensation and nuclear envelope assembly and growth.

Previous work had shown that BAF binds to DNA and to proteins containing a LEM domain, a structure that defines a family of nuclear membrane proteins. Using biochemical assays and a panel of site-directed mutants, the authors identified residues of BAF required for the protein to bind to itself, to DNA, and to emerin, a LEM-containing protein. Adding a low concentration of wild-type BAF enhances chromatin decondensation and nuclear growth in a Xenopus egg extract system, but a high concentration of BAF blocks both processes.

The results suggest that LEM-containing proteins bind to the middles of BAF dimers, while DNA binds to the left and right sides. During nuclear assembly, these interactions attach chromatin to the inner nuclear membrane, promoting chromatin decondensation and nuclear envelope growth. The availability of site-directed BAF mutants that produce a range of nuclear assembly phenotypes in the Xenopus system should provide a basis for future studies on BAF function.

Alan W. Dove

alanwdove{at}earthlink.net

CiteULike    Complore    Connotea    Del.icio.us    Digg    Facebook    Reddit    Technorati    Twitter    What's this?

Related Article

Barrier-to-autointegration factor: major roles in chromatin decondensation and nuclear assembly

Miriam Segura-Totten, Amy K. Kowalski, Robert Craigie, and Katherine L. Wilson
J. Cell Biol. 2002 158: 475-485. [Abstract] [Full Text] [PDF]

This Article Full Text (PDF, 208K) PPT slides of all figures Alert me when this article is cited Services Email this article Similar articles in this journal Alert me to new content in the JCB Download to citation manager Citing Articles Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Dove, A. W. Search for Related Content PubMed Articles by Dove, A. W. Related Collections Related Article Social Bookmarking                            What's this?