Alteration of Nuclear Lamin Organization Inhibits RNA Polymerase II-Dependent Transcription

Regulation of gene activity is mediated by alterations in chromatin organization. In addition, chromatin organization may be governed in part by interactions with structural components of the nucleus. The nuclear lamins comprise the lamina and a variety of nucleoplasmic assemblies that together are...

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Bibliographic Details
Published in:The Journal of cell biology 2002-02, Vol.156 (4), p.603-608
Main Authors: Spann, Timothy P., Goldman, Anne E., Wang, Chen, Huang, Sui, Goldman, Robert D.
Format: Article
Language:English
Subjects:
3T3 Cells
Amanitins - pharmacology
Animals
B lymphocytes
Cell aggregates
Cell Line
Cell nucleus
Cell Nucleus - metabolism
Cells
Cellular biology
Chromatin
Cricetinae
HeLa Cells
Humans
Incorporation
Lamins
Mice
Mutation
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Nucleic Acid Synthesis Inhibitors - pharmacology
Proteins
RNA
RNA Polymerase II - antagonists & inhibitors
TFIID protein
Transcription factors
Transcription, Genetic
Xenopus laevis
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Summary:Regulation of gene activity is mediated by alterations in chromatin organization. In addition, chromatin organization may be governed in part by interactions with structural components of the nucleus. The nuclear lamins comprise the lamina and a variety of nucleoplasmic assemblies that together are major structural components of the nucleus. Furthermore, lamins and lamin-associated proteins have been reported to bind chromatin. These observations suggest that the nuclear lamins may be involved in the regulation of gene activity. In this report, we test this possibility by disrupting the normal organization of nuclear lamins with a dominant negative lamin mutant lacking the NH2-terminal domain. We find that this disruption inhibits RNA polymerase II activity in both mammalian cells and transcriptionally active embryonic nuclei from Xenopus laevis. The inhibition appears to be specific for polymerase II as disruption of lamin organization does not detectably inhibit RNA polymerases I and III. Furthermore, immunofluorescence observations indicate that this selective inhibition of polymerase II-dependent transcription involves the TATA binding protein, a component of the basal transcription factor TFIID.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.200112047