Structure and chromosome mapping of the human small maf genes MAFG and MAFK

The newly emerged Maf family proteins possess a highly conserved basic leucine zipper (bZip) domain in common and are subdivided into large and small Maf proteins. The Maf family proteins appear to regulate cell differentiation processes and also cellular functions as partner molecules of CNC family proteins. To facilitate understanding of the function of small Maf proteins, we isolated the genes (MAFG and MAFK) encoding human small Maf proteins MafG and MafK and characterized their structures and organization by means of restriction enzyme mapping, Southern blot hybridization and nucleotide sequence analysis. Organization of the small maf genes are highly conserved in vertebrates, suggesting an important functional contribution of the gene products. We also examined the location of these genes within the human genome by fluorescence in situ hybridization (FISH) analysis. Human MAFG and MAFK are located at 17q25 and 7p22, respectively. Thus, small maf genes are not clustered in a single locus.

[1]  S. Orkin,et al.  The ubiquitous subunit of erythroid transcription factor NF-E2 is a small basic-leucine zipper protein related to the v-maf oncogene. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[2]  L. Peters,et al.  The ubiquitous subunit of the globin enhancer-binding protein NF-E2 (Nfe2u) maps to mouse chromosome 5. , 1994, Genomics.

[3]  K. Itoh,et al.  An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements. , 1997, Biochemical and biophysical research communications.

[4]  A. Jackson,et al.  A conserved retina-specific gene encodes a basic motif/leucine zipper domain. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[5]  J W Gray,et al.  Cytogenetic analysis using quantitative, high-sensitivity, fluorescence hybridization. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[6]  N. Andrews,et al.  Molecular characterization and localization of the human MAFG gene. , 1997, Genomics.

[7]  J. D. Engel,et al.  Mesodermal‐ vs. neuronal‐specific expression of MafK is elicited by different promoters , 1996, Genes to cells : devoted to molecular & cellular mechanisms.

[8]  K. Kataoka,et al.  Two new members of the maf oncogene family, mafK and mafF, encode nuclear b-Zip proteins lacking putative trans-activator domain. , 1993, Oncogene.

[9]  C. Kurschner,et al.  The maf proto-oncogene stimulates transcription from multiple sites in a promoter that directs Purkinje neuron-specific gene expression , 1995, Molecular and cellular biology.

[10]  A. Kolstø,et al.  Small Maf proteins interact with the human transcription factor TCF11/Nrf1/LCR-F1. , 1996, Nucleic acids research.

[11]  K. Kataoka,et al.  Maf nuclear oncoprotein recognizes sequences related to an AP-1 site and forms heterodimers with both Fos and Jun , 1994, Molecular and cellular biology.

[12]  A. Jaiswal,et al.  Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H:quinone oxidoreductase1 gene. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[13]  K. Kataoka,et al.  Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NF-E2 transcription factor , 1995, Molecular and cellular biology.

[14]  K. Kataoka,et al.  v-maf, a viral oncogene that encodes a "leucine zipper" motif. , 1989, Proceedings of the National Academy of Sciences of the United States of America.

[15]  K. Davies,et al.  Oxidative stress induces the levels of a MafG homolog in hamster HA-1 cells. , 1996, Free radical biology & medicine.

[16]  Ken Itoh,et al.  Regulation of transcription by dimerization of erythroid factor NF-E2 p45 with small Maf proteins , 1994, Nature.

[17]  N. Nomura,et al.  Human small Maf proteins form heterodimers with CNC family transcription factors and recognize the NF-E2 motif , 1997, Oncogene.