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G4 DNA Binding by LR1 and Its Subunits, Nucleolin and hnRNP D, A Role for G-G pairing in Immunoglobulin Switch Recombination
Open accessAbstract
The 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.
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Cited by
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Discovery and development of the G-rich oligonucleotide AS1411 as a novel treatment for cancer
Bates, P. J., Laber, D. A., Miller, D. M., Thomas, S. D., & Trent, J. O. (2009) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2009.01.004 · Cited by 874
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Metadata
- Authors
- Dempsey, L. A., Sun, H., Hanakahi, L. A., & Maizels, N.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-01
- Volume
- 274
- Issue
- 2
- Pages
- 1066-1071
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2132714970
- Cited by
- 188
- References
- 0
- FWCI
- 5.00
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: G4 DNA Binding by LR1 and Its Subunits, Nucleolin and hnRNP D, A Role for G-G pairing in Immunoglobulin Switch Recombination. https://app.cochat.ai/papers/10.1074/jbc.274.2.1066
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- Dempsey, L. A., Sun, H., Hanakahi, L. A., & Maizels, N. (1999). G4 DNA Binding by LR1 and Its Subunits, Nucleolin and hnRNP D, A Role for G-G pairing in Immunoglobulin Switch Recombination. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.274.2.1066
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