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The somatic V(D)J recombination for the assembly of the Ig and TCR genes is mediated by the recombination signal sequences (Rss) and the V(D)J recombinase. A cDNA clone was isolated from a lambda gt11 expression library made from mouse thymocyte poly(A)+ RNA, using the Rss as a ligand. The deduced amino acid sequence of the putative protein, designated Recognition component (Rc), reveals a pair of Cys2-His2 zinc fingers followed by a Glu- and Asp-rich acidic domain. In addition, there are five copies of the Ser/Thr-Pro-X-Arg/Lys sequence, which are putative DNA binding units. The zinc finger-acidic domain structures present in Rc are also found in several enhancer binding proteins, such as those for the kappa B motif of the Ig kappa light chain enhancer or related sequences. Bacterial fusion proteins for Rc bind preferentially to the Rss heptamer and to the kappa B motif. The dual affinities of Rc for the Rss heptamer and the kappa B motif suggest a possible link between Ig transcription and somatic recombination. The formation of multiple 'gel-shifted' DNA-protein complexes for Rc and its DNA ligand suggests that these complexes tend to multimerize.

Original publication




Journal article


Nucleic Acids Res

Publication Date





5067 - 5073


Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, DNA, DNA-Binding Proteins, Fetus, Genes, Immunoglobulin, Humans, In Situ Hybridization, Mice, Mice, Inbred BALB C, Molecular Sequence Data, Receptors, Antigen, T-Cell, Recombination, Genetic, Regulatory Sequences, Nucleic Acid, Thymus Gland, Transcription, Genetic, Zinc Fingers