The nuclear matrix maintains specific interactions with genomic DNA at sites known as matrix attachment regions (SARs). M/SARs bind in vitro to lamin polymers. We show that the polymerized α-helical rod domain of lamin Dm0 provides by itself the specific binding to the ftz M/SAR. In contrast, unpolymerized rod domain does not bind specifically to this M/ SAR. Non-specific binding to DNA is also observed with Dm0 containing a point mutation that impairs its ability to polymerize or with the isolated tail domain. These data suggests that the specific binding of lamins to M/SARs requires the rod domain and depends on the lamin polymerization state.
|Number of pages||4|
|State||Published - 12 Feb 1996|
- Drosophila melanogaster
- Nuclear lamina