c-abl has a sequence-specific enhancer binding activity

Rivka Dikstein*, Daphna Heffetz, Yinon Ben-Neriah, Yosef Shaul

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

67 Scopus citations

Abstract

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.

Original languageAmerican English
Pages (from-to)751-757
Number of pages7
JournalCell
Volume69
Issue number5
DOIs
StatePublished - 29 May 1992

Bibliographical note

Funding Information:
We thank Mordechai Anafi for providing the 543 abl-specific antisera and Dr. Jean Y. J. Wang for the gift of 8E9 monoclonal antibody. We thank Drs. Yoav Citri, Ed Harlow, Tony Hunter, Michael Karin, Michael Walker, and David Weiss and members of the laboratory for critical reading of the manuscript. This work was supported by grants from the Leo and Julia Forcheimer Center for molecular Genetics at the Weizmann institute of Science, United States-Israel Binational Science Foundation, Concern Foundation for Cancer Research (Los Angeles), Israel Cancer Research Fund, and the Research Associates of the Lautenberg Center.

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