Mutations in the lamin A/C (LMNA) gene that cause Hutchinson-Gilford progeria 
syndrome (HGPS) lead to expression of a protein called progerin with 50 amino 
acids deleted from the tail of prelamin A. In cells from patients with HGPS, 
both the amount and distribution of heterochromatin are altered. We designed in 
vitro assays to ask whether such alterations might reflect changes in chromatin, 
DNA and/or histone binding properties of progerin compared to wild-type lamin 
C-terminal tails. We show that progerin tail has a reduced DNA/chromatin binding 
capacity and modified trimethylated H3K27 binding pattern, offering a molecular 
mechanism for heterochromatin alterations related to HGPS.