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- W1931569469 abstract "By using a gel mobility retardation assay, we detected the formation of three major complexes from the binding of nuclear proteins to the promoter of the immunoglobulin lambda 2-chain gene. Two of the complexes were generated by the presence of an unidentified nuclear factor(s) called herein NF-lambda 2. Although the sequences between lambda 2- and lambda 1-chain gene promoters are very similar, the lambda 1-chain promoter did not compete for the binding of NF-lambda 2 efficiently. The binding site of NF-lambda 2 was localized by DNase I footprinting to a 14-bp region which is about 30 bp upstream of the immunoglobulin octamer motif. This region, referred to as the NF-lambda 2 motif, is within an 18-bp region of twofold rotational symmetry. Experiments with oligomers containing either the NF-lambda 2 or the octamer motifs as competitors for binding and DNase I footprinting, showed that the third complex is the product of the simultaneous binding of an octamer-binding protein and NF-lambda 2. Changing the sequence of the NF-lambda 2 motif to that of the lambda 1-chain counterpart abolished the binding ability of NF-lambda 2. Concomitantly, the level of chloramphenicol acetyltransferase expression driven by the mutated lambda 2 promoter decreased by two- to fivefold when compared with that of the wild-type promoter. It is therefore concluded that the interaction of NF-lambda 2 with the NF-lambda 2 motif stimulates transcription of the lambda 2-chain gene." @default.
- W1931569469 created "2016-06-24" @default.
- W1931569469 creator A5010708992 @default.
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- W1931569469 date "1990-11-01" @default.
- W1931569469 modified "2023-10-14" @default.
- W1931569469 title "Interaction of a nuclear protein with a palindromic sequence of the mouse immunoglobulin lambda 2-chain gene promoter is important for its transcription" @default.
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- W1931569469 doi "https://doi.org/10.1128/mcb.10.11.5894-5902.1990" @default.
- W1931569469 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/361381" @default.
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