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Figure 1


Fig. 1. Expression of wild-type and mutant lamin Dm0 constructs. (A) Schematic view of the lamin monomer, which is composed of a short N-terminal head, {alpha}-helical rod and carboxyl terminal tail domains. The major region required for binding of lamin Dm0 to chromosomes is enlarged (below) and compared with those of other species. ClustalW (http://www.ebi.ac.uk/clustalw) was used to align the sequences. Conserved residues in that region are highlighted in black (homology) or in gray (similarity). (B) The QuickChange site-directed mutagenesis method was used to produce different mutant constructs of the lamin Dm0 tail domain. These include deletions ({Delta}) and substitutions with alanine or aspartate residues. (C) Wild-type and mutant proteins were expressed, purified to near homogeneity and subjected to 12% SDS-PAGE analysis. Proteins were stained with Coomassie Brilliant Blue.





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