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J Biol Chem, Vol. 273, Issue 44, 29224-29229, October 30, 1998
From the Departments of 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.
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
,
, and
Molecular Biophysics and
Biochemistry and
Genetics, Yale University,
New Haven, Connecticut 06520-8114
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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