High impact information on MAFG

• Expressed in vitro, the hMAF protein is able to homodimerize in solution and band-shift the NFE2 tandem repeat probe [1].
• The protein, which was designated hMAF, contains a basic DNA binding domain and an extended leucine zipper but lacks any recognizable activation domain [1].
• In fact, whereas all hMAF/CNC-bZip heterodimers stimulate the activity of a gamma-promoter reporter construct in K562 cells, the association into homodimers that is induced by overexpressing hMAF inhibits the activity of the same construct [1].
• The resulting NRF3/MAFG heterodimer recognizes nuclear factor-erythroid 2/Maf recognition element-type DNA-binding motifs [2].
• In contrast, it was particularly interesting that the transcript and protein levels of the highly homologous MAFG and MAFK genes are not modulated by these cytokines [3].

Biological context of MAFG

• Structure and chromosome mapping of the human small maf-genes MAFG and MAFK [4].
• 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 [4].
• Transfection studies confirmed that NRF3 is able to dimerize with MAFG [2].
• The human MAFG gene encodes a basic-leucine zipper (bZIP) protein that belongs to a family of transcription factors related to the v-maf oncogene [5].
• We have characterized the human MAFG gene and shown that it consists of at least three exons, which are separated by small introns [5].

Other interactions of MAFG

• Human MAFG and MAFK are located at 17q25 and 7p22, respectively [4].

Analytical, diagnostic and therapeutic context of MAFG

• We have mapped the MAFG gene to human chromosome region 17q25 by fluorescence in situ hybridization [5].

References