Histone H1 binding at the 5' end of the rat albumin gene.
Biochemistry
; 23(13): 2977-83, 1984 Jun 19.
Article
en En
| MEDLINE
| ID: mdl-6087884
Cloned DNA containing the first nine exons of the rat albumin gene was digested with EcoRI and HindIII, and the resulting fragments were used to screen for regions with relatively high affinity for protein. Of three restriction fragments preferentially bound, the fragment containing the first two exons of the albumin gene was consistently bound over others by heat-stable protein extracted from liver nuclei with 0.35-1.0 M NaCl. Proteins extracted with lower and higher ionic strength buffers bound the DNA fragments, but with little specificity. The DNA fragment that was preferentially bound consistently by the 1.0 M nuclear extract was subcloned into pBR325 and was used to isolate the specific DNA-binding activity. After purification, histone H1 was the polypeptide with preferential DNA-binding activity. Histone H1 has a high-affinity binding site in the 5' end of the rat albumin gene within 440 5'-flanking base pairs and the first two exons of the gene.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
ADN
/
Albúmina Sérica
/
Histonas
/
Desoxirribonucleoproteínas
/
Genes
/
Hígado
Límite:
Animals
Idioma:
En
Revista:
Biochemistry
Año:
1984
Tipo del documento:
Article
Pais de publicación:
Estados Unidos