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Publication : LZIP-1 and LZIP-2: two novel members of the bZIP family.

First Author  Burbelo PD Year  1994
Journal  Gene Volume  139
Issue  2 Pages  241-5
PubMed ID  8112612 Mgi Jnum  J:17005
Mgi Id  MGI:65061 Doi  10.1016/0378-1119(94)90763-3
Citation  Burbelo PD, et al. (1994) LZIP-1 and LZIP-2: two novel members of the bZIP family. Gene 139(2):241-5
abstractText  A large family of bZIP proteins, containing a basic DNA-binding domain and a leucine zipper, have been described that recognize the CRE and AP-1 elements. Here, we have identified two new members, designated LZIP-1 and LZIP-2. The murine cDNA for LZIP-1 coded for a 379-amino-acid (aa) residue protein containing several distinct domains, including a Ser-rich region, a basic DNA-binding region, and an unusually long leucine zipper. A second form, LZIP-2, contained an additional 25 aa in the N-terminal region. Western immunoblotting revealed that antibody raised against part of recombinant LZIP-1 detected both forms in a variety of tissues. Gel mobility shift assays demonstrated that the recombinant protein possessed specific DNA-binding activity for both the CRE AP-1 sites. The present identification of two more ubiquitous members of the bZIP family emphasizes the complex nature of transcription factor interactions at the CRE and AP-1 sites.
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