TGGCA protein is present in erythroid nuclei and binds within the nuclease-hypersensitive sites 5' of the chicken beta H- and beta A-globin genes
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TGGCA protein is present in erythroid nuclei and binds within the nuclease-hypersensitive sites 5' of the chicken beta H- and beta A-globin genes. / Rupp, R A; Nicolas, R H; Borgmeyer, U; Lobanenkov, V V; Plumb, M A; Sippel, A E; Goodwin, G H.
in: EUR J BIOCHEM, Jahrgang 177, Nr. 3, 15.11.1988, S. 505-11.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - TGGCA protein is present in erythroid nuclei and binds within the nuclease-hypersensitive sites 5' of the chicken beta H- and beta A-globin genes
AU - Rupp, R A
AU - Nicolas, R H
AU - Borgmeyer, U
AU - Lobanenkov, V V
AU - Plumb, M A
AU - Sippel, A E
AU - Goodwin, G H
PY - 1988/11/15
Y1 - 1988/11/15
N2 - The developmentally regulated 5'-flanking DNase-I-hypersensitive site of the chicken beta H-globin gene in nuclei contains a subregion which is resistant to DNase I and which disappears when nuclei are extracted with 0.3 M NaCl, suggesting that there are salt-extractable proteins bound to sequences within this region. The 0.3 M NaCl extract contains two proteins which bind in vitro to these sequences. One of the binding sequences has an inverted repeat very similar to that bound by TGGCA protein. Partially purified TGGCA protein from chicken liver binds to this sequence in vitro giving exactly the same footprint as that obtained with erythroid nuclear proteins. Similarly TGGCA protein binds to an inverted repeat with the beta A-globin 5'-hypersensitive site giving a footprint identical to that obtained with erythroid nuclear protein extracts. From competition footprinting experiments and the electrophoretic mobility of the protein-DNA complex, it is concluded that the erythroid proteins previously described as binding to the beta H- and beta A-globin inverted repeats within the 5'-flanking hypersensitive sites both belong to the TGGCA protein family.
AB - The developmentally regulated 5'-flanking DNase-I-hypersensitive site of the chicken beta H-globin gene in nuclei contains a subregion which is resistant to DNase I and which disappears when nuclei are extracted with 0.3 M NaCl, suggesting that there are salt-extractable proteins bound to sequences within this region. The 0.3 M NaCl extract contains two proteins which bind in vitro to these sequences. One of the binding sequences has an inverted repeat very similar to that bound by TGGCA protein. Partially purified TGGCA protein from chicken liver binds to this sequence in vitro giving exactly the same footprint as that obtained with erythroid nuclear proteins. Similarly TGGCA protein binds to an inverted repeat with the beta A-globin 5'-hypersensitive site giving a footprint identical to that obtained with erythroid nuclear protein extracts. From competition footprinting experiments and the electrophoretic mobility of the protein-DNA complex, it is concluded that the erythroid proteins previously described as binding to the beta H- and beta A-globin inverted repeats within the 5'-flanking hypersensitive sites both belong to the TGGCA protein family.
KW - Animals
KW - Base Sequence
KW - Blotting, Southern
KW - CCAAT-Enhancer-Binding Proteins
KW - Cell Nucleus
KW - Chickens
KW - Chromatin
KW - DNA
KW - DNA-Binding Proteins
KW - Deoxyribonuclease I
KW - Erythrocytes
KW - Genes
KW - Globins
KW - Molecular Sequence Data
KW - NFI Transcription Factors
KW - Nuclear Proteins
KW - Plasmids
KW - Protein Binding
KW - Transcription Factors
KW - Y-Box-Binding Protein 1
M3 - SCORING: Journal article
C2 - 3197715
VL - 177
SP - 505
EP - 511
IS - 3
ER -
