| Literature DB >> 1690849 |
R A Wuerffel1, A T Nathan, A L Kenter.
Abstract
We have detected a nuclear protein from lipopolysaccharide- and dextran sulfate-stimulated mouse splenic B cells which binds specifically to the immunoglobulin switch mu (S mu) sequence. We have termed the binding protein NF-S mu. DNA containing the S mu repeated sequence, GAGCTGGGGTGAGCTGAGCTGAGCT, was used as a probe in electrophoretic mobility shift assays. Methylation interference analysis indicated that binding centers on the run of four guanine residues. Competitions with mutated S mu sequences confirmed the importance of the run of G residues and revealed that optimal binding occurs when they are flanked by GAGCT. The kinetics of the expression of NF-S mu in splenic B cells treated with lipopolysaccharide and dextran sulfate parallels the induction of recombinational activity at S mu in these cells. On the basis of these data, we suggest that NF-S mu may be an effector of switch recombination.Entities:
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Year: 1990 PMID: 1690849 PMCID: PMC362277 DOI: 10.1128/mcb.10.4.1714-1718.1990
Source DB: PubMed Journal: Mol Cell Biol ISSN: 0270-7306 Impact factor: 4.272