BZIP domain

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bZIP transcription factor
CREB.png
CREB (top) is a transcription factor capable of binding DNA via the bZIP domain (bottom) and regulating gene expression.
Identifiers
SymbolbZIP_1
Pfam PF00170
InterPro IPR011616
PROSITE PDOC00036
SCOP2 1ysa / SCOPe / SUPFAM
CDD cd14686
Membranome 235
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

The Basic Leucine Zipper Domain (bZIP 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. [1] [2]

Contents

bZIP transcription factors

bZIP transcription factors are found in all eukaryotes and form one of the largest families of dimerizing TFs. [3] An evolutionary study from 2008 revealed that 4 bZIP genes were encoded by the genome of the most recent common ancestor of all plants. [4] Interactions between bZIP transcription factors are numerous and complex [5] [6] [3] and play important roles in cancer development [7] in epithelial tissues, steroid hormone synthesis by cells of endocrine tissues, [8] factors affecting reproductive functions, [9] and several other phenomena that affect human health.

bZIP domain containing proteins

Human proteins containing this domain

ATF1; ATF2; ATF4; ATF5; ATF6; ATF7; BACH1; BACH2; BATF; BATF2; CEBPA; CEBPB; CEBPD; CEBPE; CEBPG; CEBPZ; CREB1; CREB3; CREB3L1; CREB3L2; CREB3L3; CREB3L4; CREB5; CREBL1; CREM; E4BP4; FOSL1; FOSL2; JUN; JUNB; JUND; MAFA; MAFB; MAFF; MAFG; NRL; C-MAF; MAFK; NFE2; NFE2L2; NFE2L3; SNFT; XBP1

Related Research Articles

<span class="mw-page-title-main">Basic helix–loop–helix</span> Protein structural motif

A basic helix–loop–helix (bHLH) is a protein structural motif that characterizes one of the largest families of dimerizing transcription factors. The word "basic" does not refer to complexity but to the chemistry of the motif because transcription factors in general contain basic amino acid residues in order to facilitate DNA binding.

<span class="mw-page-title-main">Leucine zipper</span> 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.

<span class="mw-page-title-main">CCAAT-enhancer-binding proteins</span> Protein family

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.

<span class="mw-page-title-main">AP-1 transcription factor</span> Instance of defined set in Homo sapiens with Reactome ID (R-HSA-6806560)

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.

<span class="mw-page-title-main">Jun dimerization protein</span> Protein-coding gene in the species Homo sapiens

Jun dimerization protein 2 (JUNDM2) is a protein that in humans is encoded by the JDP2 gene. The Jun dimerization protein is a member of the AP-1 family of transcription factors.

<span class="mw-page-title-main">NFE2L2</span> Human protein and coding gene

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 promoter regions of genes encoding cytoprotective proteins. NRF2 induces the expression of heme oxygenase 1 in vitro leading to an increase in phase II enzymes. NRF2 also inhibits the NLRP3 inflammasome.

<span class="mw-page-title-main">Sterol regulatory element-binding protein 2</span> Protein-coding gene in the species Homo sapiens

Sterol regulatory element-binding protein 2 (SREBP-2) also known as sterol regulatory element binding transcription factor 2 (SREBF2) is a protein that in humans is encoded by the SREBF2 gene.

<span class="mw-page-title-main">Activating transcription factor 2</span> Protein-coding gene in the species Homo sapiens

Activating transcription factor 2, also known as ATF2, is a protein that, in humans, is encoded by the ATF2 gene.

<span class="mw-page-title-main">USF2</span> Protein-coding gene in the species Homo sapiens

Upstream stimulatory factor 2 is a protein that in humans is encoded by the USF2 gene.

<span class="mw-page-title-main">FOSL1</span> Protein-coding gene in the species Homo sapiens

Fos-related antigen 1 (FRA1) is a protein that in humans is encoded by the FOSL1 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.

<span class="mw-page-title-main">MAFG</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">CEBPG</span> Protein-coding gene in the species Homo sapiens

CCAAT/enhancer-binding protein gamma (C/EBPγ) is a protein that in humans is encoded by the CEBPG gene. This gene has no introns.

<span class="mw-page-title-main">MAFK</span> Protein-coding gene in the species Homo sapiens

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

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

Basic leucine zipper transcription factor, ATF-like, also known as BATF, is a protein which in humans is encoded by the BATF gene.

<span class="mw-page-title-main">MAFF (gene)</span> Protein-coding gene

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

<span class="mw-page-title-main">NFE2L3</span> Protein-coding gene in the species Homo sapiens

Nuclear factor -like factor 3, also known as NFE2L3 or 'NRF3', is a transcription factor that in humans is encoded by the Nfe2l3 gene.

bZIP Maf

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 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. Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NF2-E2 transcription factor.

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. Ellenberger T (1994). "Getting a grip in DNA recognition: structures of the basic region leucine zipper, and the basic region helix-loop-helix DNA-binding domains". Curr. Opin. Struct. Biol. 4 (1): 12–21. doi:10.1016/S0959-440X(94)90054-X.
  2. Hurst HC (1995). "Transcription factors 1: bZIP proteins". Protein Profile. 2 (2): 101–68. PMID   7780801.
  3. 1 2 Amoutzias, Grigoris D.; Robertson, David L.; Van de Peer, Yves; Oliver, Stephen G. (2008-05-01). "Choose your partners: dimerization in eukaryotic transcription factors". Trends in Biochemical Sciences. 33 (5): 220–229. doi:10.1016/j.tibs.2008.02.002. ISSN   0968-0004. PMID   18406148.
  4. Corrêa LG, Riaño-Pachón DM, Schrago CG, dos Santos RV, Mueller-Roeber B, Vincentz M (2008). Shiu S (ed.). "The Role of bZIP Transcription Factors in Green Plant Evolution: Adaptive Features Emerging from Four Founder Genes". PLOS ONE. 3 (8): e2944. Bibcode:2008PLoSO...3.2944C. doi: 10.1371/journal.pone.0002944 . PMC   2492810 . PMID   18698409.
  5. Vinson, Charles; Acharya, Asha; Taparowsky, Elizabeth J. (2006-01-01). "Deciphering B-ZIP transcription factor interactions in vitro and in vivo". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1759 (1–2): 4–12. doi:10.1016/j.bbaexp.2005.12.005. ISSN   0006-3002. PMID   16580748.
  6. Newman, John R. S.; Keating, Amy E. (2003-06-27). "Comprehensive identification of human bZIP interactions with coiled-coil arrays". Science. 300 (5628): 2097–2101. Bibcode:2003Sci...300.2097N. doi: 10.1126/science.1084648 . ISSN   1095-9203. PMID   12805554. S2CID   36715183.
  7. Vlahopoulos SA, Logotheti S, Mikas D, Giarika A, Gorgoulis V, Zoumpourlis V (April 2008). "The role of ATF-2 in oncogenesis". BioEssays. 30 (4): 314–27. doi:10.1002/bies.20734. PMID   18348191. S2CID   678541.
  8. Manna PR, Dyson MT, Eubank DW, Clark BJ, Lalli E, Sassone-Corsi P, Zeleznik AJ, Stocco DM (January 2002). "Regulation of steroidogenesis and the steroidogenic acute regulatory protein by a member of the cAMP response-element binding protein family". Mol. Endocrinol. 16 (1): 184–99. doi: 10.1210/mend.16.1.0759 . PMID   11773448.
  9. Hoare S, Copland JA, Wood TG, Jeng YJ, Izban MG, Soloff MS (May 1999). "Identification of a GABP alpha/beta binding site involved in the induction of oxytocin receptor gene expression in human breast cells, potentiation by c-Fos/c-Jun". Endocrinology. 140 (5): 2268–79. doi: 10.1210/endo.140.5.6710 . PMID   10218980.