| First Author | Wu LC | Year | 1993 |
| Journal | Nucleic Acids Res | Volume | 21 |
| Issue | 22 | Pages | 5067-73 |
| PubMed ID | 8255760 | Mgi Jnum | J:15696 |
| Mgi Id | MGI:63811 | Doi | 10.1093/nar/21.22.5067 |
| Citation | Wu LC, et al. (1993) Molecular cloning of a zinc finger protein which binds to the heptamer of the signal sequence for V(D)J recombination. Nucleic Acids Res 21(22):5067-73 |
| abstractText | 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. |
