A novel cross linking technique to study nuclear lamina membrane interactions

Abstract

Protein cross-linking studies using various bifunctional reagents can provide information about the organization of complex proteinaceous structures. We have studied the association of the nuclear lamina with membrane proteins using bifunctional cross-linkers of the bis- (imidoester) class. Analysis of cross-linked products by two-dimensional diagonal gel electrophoresis demonstrates tbat the lamins are closely associated with three nuclear membrane proteins (54, 50 and 45 kDa) in intact nuclear envelopes. This interaction does not occur when the envelope organization is disrupted with detergent or urea.