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...

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Veröffentlicht in:Cell 1992-05, Vol.69 (5), p.751-757
Hauptverfasser: Dikstein, Rivka, Heffetz, Daphna, Ben-Neriah, Yinon, Shaul, Yosef
Format: Artikel
Sprache:eng
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Zusammenfassung: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.
ISSN:0092-8674
1097-4172
DOI:10.1016/0092-8674(92)90287-M