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Multiple sequence-specific DNA binding activities are eluted from chicken nuclei at low ionic strengths
Author(s) -
Mark Plumb,
Robert H. Nicolas,
Carol Wright,
Graham H. Goodwin
Publication year - 1985
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/13.11.4047
Subject(s) - biology , dna , sequence (biology) , elution , ionic bonding , base sequence , dna sequencing , binding site , dna binding protein , genetics , biochemistry , biophysics , computational biology , gene , transcription factor , chromatography , ion , chemistry , physics , quantum mechanics
DNA sequence-specific binding proteins eluted from chicken erythrocyte and thymus nuclei, and fractionated as described by Emerson and Felsenfeld (19), have been investigated by filter binding and footprint analyses. The erythrocyte nuclear protein fraction specifically binds to at least two sites within the 5' flanking chromatin hypersensitive site of the chicken beta A-globin gene, and to a site 5' to the human beta-globin gene. The major chicken beta A globin gene binding site [G)18CGGGTGG) and the human beta-globin gene binding site [TA)6(T)8C(T)4) occur at or near sequences which are hypersensitive to S1 nuclease cleavage in supercoiled plasmids. Downstream, the second chicken beta A-globin gene binding site includes the beta-globin gene CACCC consensus sequence. Filter binding studies also show other sequence specific binding activities to human N-ras and human (but not chicken) c-myc gene sequences.

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