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Specific interactions of histone H1 and a 45 kilodalton nuclear protein with a putative matrix attachment site in the distal promoter region of a cell cycle‐regulated human histone gene
Author(s) -
Pauli U.,
Chiu J. F.,
Ditullio P.,
Kroeger P.,
Shalhoub V.,
Rowe T.,
Stein G.,
Stein J.
Publication year - 1989
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041390214
Subject(s) - nuclear matrix , biology , histone h4 , nuclear protein , microbiology and biotechnology , histone , scaffold/matrix attachment region , histone h1 , gene , genetics , chromatin , transcription factor , chromatin remodeling
Protein‐DNA interactions within the promoter of a cell cycle‐regulated human H4 histone gene were examined by binding of 5′‐end‐labeled DNA segments to Western blots of nuclear protein fractions. Specific protein interactions were observed with DNA segments located between −500 bp and −1,070 bp upstream of the ATG initiation codon and included a histone H1 binding segment flanked on both sides by binding sites for a 45 kD nuclear protein. This region of the gene contains a DNase I‐sensitive site in the center (−720 to −820 bp), and sequence analysis revealed the presence of scaffold attachment sequences in the two flanking segments. Topoisomerase II consensus sequences and in vitro topoisomerase II cleavage sites were also detected in the two flanking segments. Our results suggest that the 45 kd nuclear protein may preferentially interact with these two segments of the H4 histone gene to mediate association with the nuclear matrix. The presence of negative regulatory elements in this putative matrix attachment region provides a basis for the speculation that such nuclear proteins are associated with alterations in gene‐matrix interaction that are functionally related to gene expression.