Distribution of the haptoglobin gene 5’ flanking DNA-binding nonhistone proteins in the nuclear matrix

Abstract

The nuclear matrix, a spherical proteinaceous structure consisting of the peripheral nuclear lamina with nuclear pore complexes, an extensive internal filamentous network and residual nucleoli, is obtained after the extraction of chromatin, soluble proteins and the lipoprotein nuclear membrane. .DNA loop attachment to the matrix is accomplished through contacts of specific DNA sequences, the matrix association regions (MARs) that delineate different genes and play a role in gene expression (Laemmli et al. 1992; Getzenberg 1994). In addition to MARs, there are other unique sequences on the DNA that likwise bind to the nuclear matrix (Hakes and Berezney 1991). This binding increases during elevated gene transcription (Brotherton et al. 1991; Sun et al. 1992; Poznanovic et al. 1992; 1994; 1996) asa result of a remodeling of the thee-dimensional conformation of the points of contact on the matrix due to protein redistribution and posttranslational modifications (Poznanovic et al. 1995; 1996).