Chromatin binding and silencing: Two roles of the same protein Lem2
Authors:Ramón Ramos Barrales and Sigurd Braun
doi: 10.15698/mic2016.04.495
Volume 3, pp. 185 to 188, published 04/04/2016.
Department of Physiological Chemistry, Biomedical Center, Ludwig-Maximilians-University of Munich, Grosshaderner Str. 9, 82152 Martinsried, Germany.
Keywords:
heterochromatin, perinuclear silencing, tethering, LEM, lamin-associated proteins.
Corresponding Author(s):
Conflict of interest statement:
The authors declare no competing financial interests.
Please cite this article as:
Ramón Ramos Barrales and Sigurd Braun (2016). Chromatin binding and silencing: Two roles of the same protein Lem2. Microbial Cell 3(4): 185-188. doi: 10.15698/mic2016.04.495
© 2016 Barrales and Braun. This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduction in any medium, provided the original author and source are acknowledged.
Abstract:
Transcriptionally repressed chromatin localizes to specific areas within the eukaryotic nucleus and is often found at the nuclear periphery, which is thought to provide a specialized compartment for gene silencing. However, the molecular mechanisms that establish this spatial chromatin organization are still poorly understood. In our recent work (Barrales et al. 2016), we identified the nuclear envelope protein Lem2, a homolog of metazoan lamin-associated proteins (LAPs), as a relevant factor for heterochromatin silencing and perinuclear localization in the fission yeast Schizosaccharomyces pombe. Several other LAPs have previously been reported to associate with heterochromatin, and it has been proposed that this interaction might directly contribute to gene repression, perhaps through tethering via chromatin-binding domains like the LEM domain. We demonstrated that the LEM domain of Lem2 is indeed essential for centromere binding and perinuclear tethering. However, we made the surprising finding that tethering via the LEM domain is functionally independent of Lem2’s role in silencing, which instead is mediated by a different part of the protein, the MSC domain. Our study demonstrates that tethering and silencing, although mediated by the same molecule, Lem2, can be mechanistically separated. This further unveils a complex function of this protein at the interface between the nuclear periphery and silent chromatin, which might be preserved among the other members of this conserved family of LEM proteins.