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First published online December 20, 2006

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Telling tails on chromatin and lamins

Nuclear lamins form a web-like lamina beneath the nuclear envelope. They are closely associated with chromosomes, so could regulate chromatin organization and consequently gene expression. Yosef Gruenbaum and colleagues have characterized conserved sequences in Drosophila and C. elegans lamins that might mediate this association (see p. 77). A region in the tail domain of the Drosophila B-type lamin Dm₀ binds to chromatin in vitro by interacting with histone H2A. The authors now report that a nuclear localization sequence (NLS) and a TRAT motif in this region are both required for lamin Dm₀ to bind to chromosomes. This binding requires both threonine residues in the TRAT motif, which indicates that it might be regulated by phosphorylation. The authors also show that the NLS in lamin Dm₀ and nematode lamin is required for binding to histone H2A in vitro and that lamin Dm₀ only binds to histone H2A that contains its N- and C-tail domains. These new details about chromatin-lamin interactions provide new insights into human laminopathies, since these diseases are characterized by changes in both nuclear architecture and gene regulation.

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Related articles in JCS:

Specific and conserved sequences in D. melanogaster and C. elegans lamins and histone H2A mediate the attachment of lamins to chromosomes

Anna Mattout, Michal Goldberg, Yonatan Tzur, Ayelet Margalit, and Yosef Gruenbaum
JCS 2007 120: 77-85. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?