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J Biol Chem, Vol. 273, Issue 44, 29224-29229, October 30, 1998

A Specific Isoform of hnRNP D Interacts with DNA in the LR1 Heterodimer: Canonical RNA Binding Motifs in a Sequence-specific Duplex DNA Binding Protein

Laurie A. DempseyDagger , L. A. HanakahiDagger , and Nancy MaizelsDagger parallel

From the Departments of Dagger  Molecular Biophysics and Biochemistry and parallel  Genetics, Yale University, New Haven, Connecticut 06520-8114

The B cell-specific, sequence-specific duplex DNA-binding protein LR1 is a transcriptional activator and may also function in heavy chain class switch recombination. LR1 is composed of two polypeptides, a 106-kDa subunit that is nucleolin, and a 45-kDa subunit that we now show to be a specific isoform of hnRNP D. hnRNP D and nucleolin both contain canonical RNA binding domains (RBDs also called RRMs) and Arg-Gly-Gly (RGG) motifs. Although these motifs are not commonly associated with sequence-specific recognition of duplex DNA, nonetheless LR1 binds duplex DNA with high affinity (KD = 1.8 nM) and clear sequence specificity. Two RBD-RGG proteins can therefore combine to produce a sequence-specific duplex DNA-binding protein.


Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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