Binding of matrix attachment regions to nuclear lamin is mediated by the rod domain and depends on the lamin polymerization state

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Abstract
The nuclear matrix maintains specific interactions with genomic DNA at sites known as matrix attachment regions (M/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.