Voronova, Anna and Baltimore, David (1990) Mutations that disrupt DNA binding and dimer formation in the E47 helix-loop-helix protein map to distinct domains. Proceedings of the National Academy of Sciences of the United States of America, 87 (12). pp. 4722-4726. ISSN 0027-8424 http://resolver.caltech.edu/CaltechAUTHORS:20120425-134250382
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A common DNA binding and dimerization domain containing an apparent "helix-loop-helix" (HLH) structure was recognized recently in a number of regulatory proteins, including the E47 and E12 proteins that bind to the kappa E2 motif in immunoglobulin kappa gene enhancer. The effect of site-directed mutagenesis on E47 protein multimerization and DNA binding was examined. Mutations in either putative helix domain disrupted protein dimerization and DNA binding. No DNA binding was observed when mutations were introduced in the basic region, but these mutants were able to dimerize. These basic region mutants were not able to bind to DNA as heterodimers with the wild-type E47 proteins, demonstrating that two functional basic regions are required for binding to DNA. Therefore the basic region mutants are "transdominant."
|Additional Information:||© 1990 National Academy of Sciences. Contributed by David Baltimore, April 2, 1990. We thank Cornelis Murre, Mark Kamps, Richard Van Etten, and Sankar Ghosh for helpful advice and discussion. We also thank Robert Weinberg and Dan Silver for reading the manuscript. A.V. is supported by a postdoctoral fellowship from The American Cancer Society. This work was supported by U.S. Public Health Service Grant GM 39458. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.|
|Subject Keywords:||HLH, helix-loop-helix; EMSA, electrophoretic mobility shift assay|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Jason Perez|
|Deposited On:||26 Apr 2012 20:54|
|Last Modified:||26 Apr 2012 20:54|
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