LZIP-1 and LZIP-2: two novel members of the bZIP family.
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.
Burbelo
P D
PD
Laboratory of Developmental Biology, National Institute of Dental Research, National Institutes of Health, Bethesda, MD 20892.
Gabriel
G C
GC
Kibbey
M C
MC
Yamada
Y
Y
Kleinman
H K
HK
Weeks
B S
BS
D000818:Animals; D001483:Base Sequence; D002460:Cell Line; D004268:DNA-Binding Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D005347:Fibroblasts; D016350:Leucine Zippers / Q000235:genetics*; D008546:Melanoma, Experimental / Q000737:chemistry / Q000235:genetics; D051379:Mice; D008969:Molecular Sequence Data; D014157:Transcription Factors / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism
D004268:DNA-Binding Proteins; D014157:Transcription Factors