c-abl has a sequence-specific enhancer binding activity.
The enhancers of several distinct viruses contain a common functional element, termed EP. This element binds ubiquitous cellular proteins and generates specific complexes in gel retardation analysis. Ultraviolet cross-linking and Southwestern analysis showed that a 140 kd polypeptide is the major EP DNA-binding protein. Using a combination of DNA binding and immunological techniques, we have identified the c-abl protein in a nuclear complex that binds to the EP element. abl was found to have both a specific and high affinity DNA binding activity. The ability to bind DNA is abolished in the mutant abl protein, p210bcr-abl, consistent with its cytoplasmic localization in chronic myelogenous leukemia.
Dikstein
R
R
Department of Molecular Genetics and Virology, Weizmann Institute of Science, Rehovot, Israel.
Heffetz
D
D
Ben-Neriah
Y
Y
Shaul
Y
Y
D001483:Base Sequence; D015342:DNA Probes / Q000235:genetics; D004279:DNA, Viral / Q000378:metabolism*; D004742:Enhancer Elements, Genetic / Q000235:genetics*; D016313:Genes, abl; D006367:HeLa Cells; D006515:Hepatitis B virus / Q000235:genetics; D006801:Humans; D008969:Molecular Sequence Data; D011233:Precipitin Tests; D016315:Proto-Oncogene Proteins c-abl / Q000235:genetics / Q000378:metabolism*
D015342:DNA Probes; D004279:DNA, Viral; D016315:Proto-Oncogene Proteins c-abl