The major human erythroid DNA-binding protein (GF-1): Primary sequence and localization of the gene to the X chromosome
Journal Article
·
· Proceedings of the National Academy of Sciences of the United States of America; (USA)
- Harvard Medical School, Boston, MA (USA) Howard Hughes Medical Institute, Boston, MA (USA)
- Massachusetts Institute of Technology, Cambridge (USA)
- Harvard Medical School, Boston, MA (USA)
Genes expressed in erythroid cells contain binding sites for a cell-specific nuclear factor, GF-1 (NF-E1, Eryf 1), believed to be an important transcriptional regulator. Previously the authors characterized murine GF-1 as a 413-amino acid polypeptide containing two cysteine-cysteine regions reminiscent of zinc-finger DNA-binding domains. By cross-hybridization to the finger domain of murine GF-1 they have isolated cDNA encoding the human homolog. Peptide sequencing of purified human GF-1 confirmed the authenticity of the human cDNA. The predicted primary sequence of human GF-1 is highly similar to that of murine GF-1, particularly in the DNA-binding region. Although the DNA-binding domains of human, murine, and chicken proteins are remarkably conserved, the mammalian polypeptides are strikingly divergent from the avian counterpart in other regions, most likely those responsible for transcriptional activation. By hybridization to panels of human-rodent DNAs they have assigned the human GF-1 locus to Xp21-11. The localization of the gene to the X chromosome has important implications for hereditary persistence of fetal hemoglobin syndromes unlinked to the {beta}-globin cluster and for genetic experiments designed to test the role of the factor in erythroid cell gene expression.
- OSTI ID:
- 6718404
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America; (USA), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (USA) Vol. 87:2; ISSN PNASA; ISSN 0027-8424
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
550201* -- Biochemistry-- Tracer Techniques
550401 -- Genetics-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMINO ACID SEQUENCE
AMINO ACIDS
ANIMALS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
CARBOXYLIC ACIDS
CHROMOSOMES
CYSTEINE
DAYS LIVING RADIOISOTOPES
DISEASES
DNA
DNA HYBRIDIZATION
DNA SEQUENCING
GENETIC MAPPING
GLOBIN
GLOBINS
HEMOGLOBIN
HEREDITARY DISEASES
HETEROCHROMOSOMES
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
HUMAN X CHROMOSOME
HYBRIDIZATION
ISOTOPES
LIGHT NUCLEI
MAMMALS
MAN
MAPPING
MOLECULAR STRUCTURE
NUCLEI
NUCLEIC ACIDS
NUCLEOPROTEINS
ODD-ODD NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
ORGANIC SULFUR COMPOUNDS
PHOSPHORUS 32
PHOSPHORUS ISOTOPES
PIGMENTS
PORPHYRINS
PRIMATES
PROTEINS
RADIOISOTOPES
RECOMBINANT DNA
STRUCTURAL CHEMICAL ANALYSIS
THIOLS
TRANSCRIPTION FACTORS
VERTEBRATES
X CHROMOSOME
550401 -- Genetics-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMINO ACID SEQUENCE
AMINO ACIDS
ANIMALS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
CARBOXYLIC ACIDS
CHROMOSOMES
CYSTEINE
DAYS LIVING RADIOISOTOPES
DISEASES
DNA
DNA HYBRIDIZATION
DNA SEQUENCING
GENETIC MAPPING
GLOBIN
GLOBINS
HEMOGLOBIN
HEREDITARY DISEASES
HETEROCHROMOSOMES
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
HUMAN X CHROMOSOME
HYBRIDIZATION
ISOTOPES
LIGHT NUCLEI
MAMMALS
MAN
MAPPING
MOLECULAR STRUCTURE
NUCLEI
NUCLEIC ACIDS
NUCLEOPROTEINS
ODD-ODD NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
ORGANIC SULFUR COMPOUNDS
PHOSPHORUS 32
PHOSPHORUS ISOTOPES
PIGMENTS
PORPHYRINS
PRIMATES
PROTEINS
RADIOISOTOPES
RECOMBINANT DNA
STRUCTURAL CHEMICAL ANALYSIS
THIOLS
TRANSCRIPTION FACTORS
VERTEBRATES
X CHROMOSOME