Molecular Cloning of a Putative Novel Human bZIP Transcription Factor on Chromosome 17q22

Luna, Luisa; Johnsen, Øyvind; Skartlien, Anne Helen; Pédeutour, Florence; Turc‐Carel, Claude; Prydz, Hans; Kolstø, Anne‐Brit

doi:10.1006/geno.1994.1428

Cited by 84 publications

(72 citation statements)

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“…Therefore, Ech-small Maf heterodimers may be functionally more important than p45-small Maf heterodimers in activating erythroid cell-specific gene expression and regulating hematopoietic cell differentiation. In addition, two other p45-related molecules, Nrf1/LCR-F1/TCF11 (6,8,30) and Nrf2 (35), have been identified. These two molecules show ubiquitous expression patterns but may play some regulatory role in hematopoietic cellspecific gene expression.…”

Section: Discussionmentioning

confidence: 99%

“…A transient increase of Fos in response to growth-stimulatory signals could modify the binding specificities of small Maf proteins. Alternatively, ubiquitously expressed p45-related molecules such as Nrf1/LCR-F1/TCF11 (6)(7)(8)30) and Nrf2 (35) may act as heterodimeric partners of the small Maf proteins. Since these molecules do not efficiently form homodimers and are significantly homologous with p45, it seems likely that these molecules also form heterodimers with the small Maf proteins and specify the binding of the heterodimers to DNA sequences related to the NF-E2 site.…”

Section: Discussionmentioning

confidence: 99%

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Small Maf Proteins Heterodimerize with Fos and May Act as Competitive Repressors of the NF-E2 Transcription Factor

Kataoka

Igarashi

Itoh

et al. 1995

Molecular and Cellular Biology

211

169

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The maf oncogene encodes a bZip nuclear protein which recognizes sequences related to an AP-1 site either as a homodimer or as heterodimers with Fos and Jun. We describe here a novel maf-related gene, mafG, which shows extensive homology with two other maf-related genes, mafK and mafF. These three maf-related genes encode small basic-leucine zipper proteins lacking the trans-activator domain of v-Maf. Bacterially expressed small Maf proteins bind to DNA as homodimers with a sequence recognition profile that is virtually identical to that of v-Maf. As we have previously described, the three small Maf proteins also dimerize with the large subunit of NF-E2 (p45) to form an erythroid cell-specific transcription factor, NF-E2, which has distinct DNA-binding specificity. This study shows that the small Maf proteins can also dimerize among themselves and with Fos and a newly identified p45-related molecule (Ech) but not with v-Maf or Jun. Although the small Maf proteins preferentially recognize the consensus NF-E2 sequence as heterodimers with either NF-E2 p45, Ech, or Fos, these heterodimers seemed to be different in their transactivation potentials. Coexpression of Fos and small Mafs could not activate a promoter with tandem repeats of the NF-E2 site. These results raise the possibility that tissue-specific gene expression and differentiation of erythroid cells are regulated by competition among Fos, NF-E2 p45, and Ech for small Maf proteins and for binding sites.The maf oncogene was identified by structural analysis of the genome of the AS42 avian transforming retrovirus (26,40). It encodes a nuclear basic-leucine zipper (bZip) protein which can form a homodimer through its zipper structure (23). Recently, we reported that the v-Maf homodimer specifically recognizes two relatively long palindromic DNA sequences, TGCTGACTCAGCA and TGCTGACGTCAGCA, at roughly equal efficiency (24). The middle parts of the two consensus binding sequences for Maf are identical with two well-characterized binding sequences of the AP-1 transcription factor, the 12-O-tetradecanoylphorbol-13-acetate (TPA)-responsive element (TRE; TGACTCA) and the cyclic AMP-responsive element (CRE; TGACGTCA), respectively. We therefore named the two types of recognition elements TRE-type Maf recognition elements (MAREs) and CRE-type MAREs. It was also recently revealed that Maf forms heterodimers with the two major components of AP-1, Fos and Jun (24, 27, 28). These heterodimers preferably bind to asymmetric DNA sequences consisting of the two consensus binding sequences of Maf homodimer and AP-1 (24). Thus, Maf and the two AP-1 components are suggested to interact with each other in a cooperative or inhibitory way in association with their recognition sequences by forming heterodimers of altered binding specificities.Like many other proto-oncogenes, the c-maf gene is a member of a gene family. To date, four maf-related genes, mafK, mafF, mafB, and nrl, have been reported (14,22,53). Their gene products are closely related to v-Maf especially in the structur...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Small Maf Proteins Heterodimerize with Fos and May Act as Competitive Repressors of the NF-E2 Transcription Factor

Kataoka

Igarashi

Itoh

et al. 1995

Molecular and Cellular Biology

211

169

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“…Recently, new CNC family members, Nrf1 (Caterina et al, 1994;Chan et al, 1993b;Luna et al, 1994) and Nrf2 (Moi et al, 1994) were identi®ed in human erythroleukemic cell lines. Nrf1 has been shown to be a potent transcriptional activator in erythroid cells, as compared with p45 (Caterina et al, 1994).…”

Section: Mafk and Mafg Bind To Nf-e2 Sites By Forming Heterodimers Wimentioning

confidence: 99%

“…MafK has been shown to be an authentic subunit of murine NF-E2 (Andrews et al, 1993a;Igarashi et al, 1995a). In man, two other CNC family proteins, Nrf1/LCR-F1/TCF11 (Caterina et al, 1994;Chan et al, 1993b;Luna et al, 1994) and Nrf2 (Moi et al, 1994) have been identi®ed, although their DNA binding activities have not been characterized in detail.…”

Section: Introductionmentioning

confidence: 99%

“…These data suggest that p45 and its dimeric partner molecules play vital roles in both normal di erentiation of hematopoietic cells and leukemic transformation. However, in man, while CNC family members have been cloned and characterized (Ney et al, 1993;Chan et al, 1993a;Luna et al, 1994), none of the small Maf family proteins have so far been isolated.…”

Section: Introductionmentioning

confidence: 99%

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Human small Maf proteins form heterodimers with CNC family transcription factors and recognize the NF-E2 motif

et al. 1997

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The transcription factor NF-E2, a heterodimeric protein complex composed of p45 and small Maf family proteins, is considered crucial for the regulation of erythroid gene expression and platelet formation. To facilitate the characterization of NF-E2 functions in human cells, we isolated cDNAs encoding two members of the small Maf family, MafK and MafG. The human mafK and mafG genes encode proteins of 156 and 162 amino acid residues, respectively, whose deduced amino acid sequences show approximately 95% identity to their respective chicken counterparts. Expression of mafK mRNA is high in heart, skeletal muscle and placenta, whereas mafG mRNA is abundant in skeletal muscle and is moderately expressed in heart and brain. Both are expressed in all hematopoietic cell lines, including those of erythroid and megakaryocytic lineages. In electrophoretic gel mobility shift assays binding to NF-E2 sites was found to depend on formation of homodimers or heterodimers with p45 and p45-related CNC family proteins. The results suggest that the small Maf family proteins function in human cells through interaction with various basic-leucine zipper-type transcription factors.

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Structure of the supernumerary ring and giant rod chromosomes in adipose tissue tumors

Pédeutour

Forus

Coindre

et al. 1999

Genes Chromosom. Cancer

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242

126

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Molecular Cloning of a Putative Novel Human bZIP Transcription Factor on Chromosome 17q22

Cited by 84 publications

References 0 publications

Small Maf Proteins Heterodimerize with Fos and May Act as Competitive Repressors of the NF-E2 Transcription Factor

Small Maf Proteins Heterodimerize with Fos and May Act as Competitive Repressors of the NF-E2 Transcription Factor

Human small Maf proteins form heterodimers with CNC family transcription factors and recognize the NF-E2 motif

Structure of the supernumerary ring and giant rod chromosomes in adipose tissue tumors

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