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pubmed-article:9873052pubmed:abstractTextThe immunoglobulin heavy chain switch regions contain multiple runs of guanines on the top (nontemplate) DNA strand. Here we show that LR1, a B cell-specific, duplex DNA binding factor, binds tightly and specifically to synthetic oligonucleotides containing G-G base pairs (KD </= 0.25 nM). LR1 also binds to single-stranded G-rich sequences (KD approximately 10 nM). The two subunits of LR1, nucleolin and hnRNP D, bind with high affinity to G4 DNA (KD = 0.4 and 0.5 nM, respectively). LR1 therefore contains two independent G4 DNA binding domains. We propose that LR1 binds with G-G-paired structures that form during the transcription of the S regions that is prerequisite to recombination in vivo. Interactions of donor and acceptor S regions with subunits of the LR1 could then juxtapose the switch regions for recombination.lld:pubmed
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pubmed-article:9873052pubmed:articleTitleG4 DNA binding by LR1 and its subunits, nucleolin and hnRNP D, A role for G-G pairing in immunoglobulin switch recombination.lld:pubmed
pubmed-article:9873052pubmed:affiliationDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8114, USA.lld:pubmed
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pubmed-article:9873052pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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