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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Barrales, Ramón Ramos Forn, Marta Georgescu, Paula Raluca Sarkadi, Zsuzsa Braun, Sigurd |
| Description | Author Affiliation: Barrales RR ( Department of Physiological Chemistry, Biomedical Center, Ludwig-Maximilians-University of Munich, 82152 Martinsried, Germany); Forn M ( Department of Physiological Chemistry, Biomedical Center, Ludwig-Maximilians-University of Munich, 82152 Martinsried, Germany); Georgescu PR ( Department of Physiological Chemistry, Biomedical Center, Ludwig-Maximilians-University of Munich, 82152 Martinsried, Germany); Sarkadi Z ( Department of Physiological Chemistry, Biomedical Center, Ludwig-Maximilians-University of Munich, 82152 Martinsried, Germany); Braun S ( Department of Physiological Chemistry, Biomedical Center, Ludwig-Maximilians-University of Munich, 82152 Martinsried, Germany) |
| Abstract | Transcriptionally silent chromatin localizes to the nuclear periphery, which provides a special microenvironment for gene repression. A variety of nuclear membrane proteins interact with repressed chromatin, yet the functional role of these interactions remains poorly understood. Here, we show that, in Schizosaccharomyces pombe, the nuclear membrane protein Lem2 associates with chromatin and mediates silencing and heterochromatin localization. Unexpectedly, we found that these functions can be separated and assigned to different structural domains within Lem2, excluding a simple tethering mechanism. Chromatin association and tethering of centromeres to the periphery are mediated by the N-terminal LEM (LAP2-Emerin-MAN1) domain of Lem2, whereas telomere anchoring and heterochromatin silencing require exclusively its conserved C-terminal MSC (MAN1-Src1 C-terminal) domain. Particularly, silencing by Lem2 is epistatic with the Snf2/HDAC (histone deacetylase) repressor complex SHREC at telomeres, while its necessity can be bypassed by deleting Epe1, a JmjC protein with anti-silencing activity. Furthermore, we found that loss of Lem2 reduces heterochromatin association of SHREC, which is accompanied by increased binding of Epe1. This reveals a critical function of Lem2 in coordinating these antagonistic factors at heterochromatin. The distinct silencing and localization functions mediated by Lem2 suggest that these conserved LEM-containing proteins go beyond simple tethering to play active roles in perinuclear silencing. |
| File Format | HTM / HTML |
| ISSN | 08909369 |
| e-ISSN | 15495477 |
| DOI | 10.1101/gad.271288.115 |
| Journal | Genes & Development |
| Issue Number | 2 |
| Volume Number | 30 |
| Language | English |
| Publisher | Cold Spring Harbor Laboratory Press |
| Publisher Date | 2016-01-15 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Discipline Molecular Discipline Biology__semicolon__developmental Discipline Biology__semicolon__genetics__semicolon__cell Discipline Biology Heterochromatin Metabolism Nuclear Proteins Schizosaccharomyces Pombe Proteins Gene Deletion Gene Silencing Genetics Protein Binding Protein Structure, Tertiary Protein Transport Schizosaccharomyces Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Genetics Developmental Biology |
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