BZIP Maf

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bZIP_Maf
Crystal structure of the MafA homodimer.png
Crystal structure of the MafA homodimer bound to DNA. PDB entry 3a5t [1]
Identifiers
SymbolbZIP_Maf
Pfam PF03131
Pfam clan CL0018
InterPro IPR004826
SCOP2 1k1v / SCOPe / SUPFAM

bZIP Maf is a domain found in Maf transcription factor proteins. It contains a leucine zipper (bZIP) domain, which mediates the transcription factor's dimerization and DNA binding properties. The Maf extended homology region (EHR) is present at the N-terminus of the protein. This region (shown in yellow in the adjacent image) exists only within the Maf family and allows the family to recognize longer DNA motifs than other leucine zippers. These motifs are termed the Maf recognition element (MARE) and is 13 or 14 base pairs long. In particular, the two residues at the beginning of helix H2 are positioned to recognise the flanking region of the DNA. [2] Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NF2-E2 transcription factor.

In mouse, Maf1 may play an early role in axial patterning. Defects in these proteins are a cause of autosomal dominant retinitis pigmentosa. Neural retina-specific leucine zipper proteins belong to this family.

Related Research Articles

Leucine zipper DNA-binding structural motif

A leucine zipper is a common three-dimensional structural motif in proteins. They were first described by Landschulz and collaborators in 1988 when they found that an enhancer binding protein had a very characteristic 30-amino acid segment and the display of these amino acid sequences on an idealized alpha helix revealed a periodic repetition of leucine residues at every seventh position over a distance covering eight helical turns. The polypeptide segments containing these periodic arrays of leucine residues were proposed to exist in an alpha-helical conformation and the leucine side chains from one alpha helix interdigitate with those from the alpha helix of a second polypeptide, facilitating dimerization.

A DNA-binding domain (DBD) is an independently folded protein domain that contains at least one structural motif that recognizes double- or single-stranded DNA. A DBD can recognize a specific DNA sequence or have a general affinity to DNA. Some DNA-binding domains may also include nucleic acids in their folded structure.

CCAAT-enhancer-binding proteins

CCAAT-enhancer-binding proteins is a family of transcription factors composed of six members, named from C/EBPα to C/EBPζ. They promote the expression of certain genes through interaction with their promoters. Once bound to DNA, C/EBPs can recruit so-called co-activators that in turn can open up chromatin structure or recruit basal transcription factors.

AP-1 transcription factor

Activator protein 1 (AP-1) is a transcription factor that regulates gene expression in response to a variety of stimuli, including cytokines, growth factors, stress, and bacterial and viral infections. AP-1 controls a number of cellular processes including differentiation, proliferation, and apoptosis. The structure of AP-1 is a heterodimer composed of proteins belonging to the c-Fos, c-Jun, ATF and JDP families.

NFE2L2

Nuclear factor erythroid 2-related factor 2 (NRF2), also known as nuclear factor erythroid-derived 2-like 2, is a transcription factor that in humans is encoded by the NFE2L2 gene. NRF2 is a basic leucine zipper (bZIP) protein that may regulate the expression of antioxidant proteins that protect against oxidative damage triggered by injury and inflammation, according to preliminary research. In vitro, NRF2 binds to antioxidant response elements (AREs) in the nucleus leading to transcription of ARE genes. NRF2 increases heme oxygenase 1 leading to an increase in phase II enzymes in vitro. NRF2 also inhibits the NLRP3 inflammasome.

ATF1

Cyclic AMP-dependent transcription factor ATF-1 is a protein that in humans is encoded by the ATF1 gene.

ATF4

Activating transcription factor 4 , also known as ATF4, is a protein that in humans is encoded by the ATF4 gene.

ATF6

Activating transcription factor 6, also known as ATF6, is a protein that, in humans, is encoded by the ATF6 gene and is involved in the unfolded protein response.

BACH1

Transcription regulator protein BACH1 is a protein that in humans is encoded by the BACH1 gene.

MAF (gene)

Transcription factor Maf also known as proto-oncogene c-Maf or V-maf musculoaponeurotic fibrosarcoma oncogene homolog is a transcription factor that in humans is encoded by the MAF gene.

<i>NRL</i> (gene) Protein-coding gene in the species Homo sapiens

Neural retina-specific leucine zipper protein is a protein that in humans is encoded by the NRL gene.

MAFG

Transcription factor MafG is a bZip Maf transcription factor protein that in humans is encoded by the MAFG gene.

NFE2L1

Nuclear factor erythroid 2-related factor 1 (Nrf1) also known as nuclear factor erythroid-2-like 1 (NFE2L1) is a protein that in humans is encoded by the NFE2L1 gene. Since NFE2L1 is referred to as Nrf1, it is often confused with nuclear respiratory factor 1 (Nrf1).

CEBPG

CCAAT/enhancer-binding protein gamma is a protein that in humans is encoded by the CEBPG gene.

BACH2

Transcription regulator protein BACH2 is a protein that in humans is encoded by the BACH2 gene. It contains a BTB/POZ domain at its N-terminus which forms a disulphide-linked dimer and a bZip_Maf domain at the C-terminus.

TEF (gene)

Thyrotroph embryonic factor is a protein that in humans is encoded by the TEF gene.

MAFK

Transcription factor MafK is a bZip Maf transcription factor protein that in humans is encoded by the MAFK gene.

MAFF (gene)

Transcription factor MafF is a bZip Maf transcription factor protein that in humans is encoded by the MAFF gene.

bZIP domain

The Basic Leucine Zipper Domain is found in many DNA binding eukaryotic proteins. One part of the domain contains a region that mediates sequence specific DNA binding properties and the leucine zipper that is required to hold together (dimerize) two DNA binding regions. The DNA binding region comprises a number of basic amino acids such as arginine and lysine. Proteins containing this domain are transcription factors.

Small Maf proteins are basic region leucine zipper-type transcription factors that can bind to DNA and regulate gene regulation. There are three small Maf (sMaf) proteins, namely MafF, MafG, and MafK, in vertebrates. HUGO Gene Nomenclature Committee (HGNC)-approved gene names of MAFF, MAFG and MAFK are “v-maf avian musculoaponeurotic fibrosarcoma oncogene homolog F, G, and K”, respectively.

References

  1. Kurokawa, H.; Motohashi, H.; Sueno, S.; Kimura, M.; Takagawa, H.; Kanno, Y.; Yamamoto, M.; Tanaka, T. (2009). "Structural Basis of Alternative DNA Recognition by Maf Transcription Factors". Molecular and Cellular Biology. 29 (23): 6232–6244. doi:10.1128/MCB.00708-09. PMC   2786689 . PMID   19797082.
  2. Kusunoki H, Motohashi H, Katsuoka F, Morohashi A, Yamamoto M, Tanaka T (April 2002). "Solution structure of the DNA-binding domain of MafG". Nat. Struct. Biol. 9 (4): 252–6. doi:10.1038/nsb771. PMID   11875518. S2CID   23687470.
This article incorporates text from the public domain Pfam and InterPro: IPR004826