The tail domain of lamin Dm0 binds histones H2A and H2B
- Michal Goldberg*,†,
- Amnon Harel*,†,‡,
- Michael Brandeis*,
- Thomas Rechsteiner§,
- Timothy J. Richmond§,
- Aryeh M. Weiss¶, and
- Yosef Gruenbaum*,‖
- *Department of Genetics, The Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem 91904, Israel; §Institut fur Molekularbiologie und Biophysik, Eidgenössiche Technische Hochschule-Hoenggerberg, Zürich CH-8093, Switzerland; and ¶Department of Electronics, Jerusalem College of Technology, Jerusalem 91160, Israel
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Edited by Roger D. Kornberg, Stanford University School of Medicine, Stanford, CA, and approved January 10, 1999 (received for review November 20, 1998)
Abstract
In multicellular organisms, the higher order organization of chromatin during interphase and the reassembly of the nuclear envelope during mitosis are thought to involve an interaction between the nuclear lamina and chromatin. The nuclear distribution of lamins and of peripheral chromatin is highly correlated in vivo, and lamins bind specifically to chromatin in vitro. Deletion mutants of Drosophila lamin Dm0 were expressed to map regions of the protein that are required for its binding to chromosomes. The binding activity requires two regions in the lamin Dm0 tail domain. The apparent K d of binding of the lamin Dm0 tail domain was found to be approximately 1 μM. Chromatin subfractions were examined to search for possible target molecules for the binding of lamin Dm0. Isolated polynucleosomes, nucleosomes, histone octamer, histone H2A/H2B dimer, and histones H2A or H2B displaced the binding of lamin Dm0 tail to chromosomes. This displacement was specific, because polyamines or proteins such as histones H1, H3, or H4 did not displace the binding of the lamin Dm0 tail to chromosomes. In addition, DNA sequences, including M/SARs, did not interfere with the binding of lamin Dm0 tail domain to chromosomes. Taken together, these results suggest that the interaction between the tail domain of lamin Dm0 and histones H2A and H2B may mediate the attachment of the nuclear lamina to chromosomes in vivo.
Footnotes
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↵ † M.G. and A.H. contributed equally to this work.
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↵ ‡ Present address: Department of Biology, University of California at San Diego, La Jolla, CA.
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↵ ‖ To whom reprint requests should be addressed. e-mail: gru{at}vms.huji.ac.il.
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This paper was submitted directly (Track II) to the Proceedings Office.
- Copyright © 1999, The National Academy of Sciences
