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16  structures 134  species 1  interaction 729  sequences 57  architectures

Family: zf-TAZ (PF02135)

Summary: TAZ zinc finger

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This is the Wikipedia entry entitled "TAZ zinc finger". More...

TAZ zinc finger Edit Wikipedia article

zf-TAZ
PDB 1f81 EBI.jpg
solution structure of the taz2 domain of the transcriptional adaptor protein cbp
Identifiers
Symbol zf-TAZ
Pfam PF02135
InterPro IPR000197
SCOP 1f81
SUPERFAMILY 1f81

In molecular biology, TAZ zinc finger (Transcription Adaptor putative Zinc finger) domains are zinc-containing domains found in the homologous transcriptional co-activators CREB-binding protein (CBP) and the P300. CBP and P300 are histone acetyltransferases (EC) that catalyse the reversible acetylation of all four histones in nucleosomes, acting to regulate transcription via chromatin remodelling. These large nuclear proteins interact with numerous transcription factors and viral oncoproteins, including p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1, and are involved in cell growth, differentiation and apoptosis.[1] Both CBP and P300 have two copies of the TAZ domain, one in the N-terminal region, the other in the C-terminal region. The TAZ1 domain of CBP and P300 forms a complex with CITED2 (CBP/P300-interacting transactivator with ED-rich tail), inhibiting the activity of the hypoxia inducible factor (HIF-1alpha) and thereby attenuating the cellular response to low tissue oxygen concentration.[2] Adaptation to hypoxia is mediated by transactivation of hypoxia-responsive genes by hypoxia-inducible factor-1 (HIF-1) in complex with the CBP and p300 transcriptional coactivators.[3]

The TAZ domain adopts an all-alpha fold with zinc-binding sites in the loops connecting the helices. The TAZ1 domain in P300 and the TAZ2 (CH3) domain in CBP have each been shown to have four amphipathic helices, organised by three zinc-binding clusters with HCCC-type coordination.[4][5][6]

References[edit]

  1. ^ Ponting CP, Blake DJ, Davies KE, Kendrick-Jones J, Winder SJ (January 1996). "ZZ and TAZ: new putative zinc fingers in dystrophin and other proteins". Trends Biochem. Sci. 21 (1): 11–13. PMID 8848831. 
  2. ^ Freedman SJ, Sun ZY, Kung AL, France DS, Wagner G, Eck MJ (July 2003). "Structural basis for negative regulation of hypoxia-inducible factor-1alpha by CITED2". Nat. Struct. Biol. 10 (7): 504–12. doi:10.1038/nsb936. PMID 12778114. 
  3. ^ Freedman SJ, Sun ZY, Poy F, Kung AL, Livingston DM, Wagner G, Eck MJ (April 2002). "Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha". Proc. Natl. Acad. Sci. U.S.A. 99 (8): 5367–72. doi:10.1073/pnas.082117899. PMC 122775. PMID 11959990. 
  4. ^ De Guzman RN, Liu HY, Martinez-Yamout M, Dyson HJ, Wright PE (October 2000). "Solution structure of the TAZ2 (CH3) domain of the transcriptional adaptor protein CBP". J. Mol. Biol. 303 (2): 243–53. doi:10.1006/jmbi.2000.4141. PMID 11023789. 
  5. ^ De Guzman RN, Martinez-Yamout MA, Dyson HJ, Wright PE (January 2004). "Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites". J. Biol. Chem. 279 (4): 3042–9. doi:10.1074/jbc.M310348200. PMID 14594809. 
  6. ^ De Guzman RN, Wojciak JM, Martinez-Yamout MA, Dyson HJ, Wright PE (January 2005). "CBP/p300 TAZ1 domain forms a structured scaffold for ligand binding". Biochemistry 44 (2): 490–7. doi:10.1021/bi048161t. PMID 15641773. 

This article incorporates text from the public domain Pfam and InterPro IPR000197

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

TAZ zinc finger Provide feedback

The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC.

Literature references

  1. De Guzman RN, Liu HY, Martinez-Yamout M, Dyson HJ, Wright PE; , J Mol Biol 2000;303:243-253.: Solution structure of the TAZ2 (CH3) domain of the transcriptional adaptor protein CBP PUBMED:11023789 EPMC:11023789

  2. Goto NK, Zor T, Martinez-Yamout M, Dyson HJ, Wright PE; , J Biol Chem 2002;277:43168-43174.: Cooperativity in transcription factor binding to the coactivator CREB-binding protein (CBP). The mixed lineage leukemia protein (MLL) activation domain binds to an allosteric site on the KIX domain. PUBMED:12205094 EPMC:12205094

  3. De Guzman RN, Martinez-Yamout MA, Dyson HJ, Wright PE; , 0;0:0-0.: Interaction of the TAZ1 domain of CREB-binding protein with the activation domain of CITED2: Regulation by competition between intrinsically unstructured ligands for non-identical binding sites. PUBMED:14594809 EPMC:14594809

  4. Dames SA, Martinez-Yamout M, De Guzman RN, Dyson HJ, Wright PE; , Proc Natl Acad Sci U S A 2002;99:5271-5276.: Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response. PUBMED:11959977 EPMC:11959977


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000197

Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [PUBMED:10529348, PUBMED:15963892, PUBMED:15718139, PUBMED:17210253, PUBMED:12665246]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few [PUBMED:11179890]. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.

TAZ (Transcription Adaptor putative Zinc finger) domains are zinc-containing domains found in the homologous transcriptional co-activators CREB-binding protein (CBP) and the P300. CBP and P300 are histone acetyltransferases (EC) that catalyse the reversible acetylation of all four histones in nucleosomes, acting to regulate transcription via chromatin remodelling. These large nuclear proteins interact with numerous transcription factors and viral oncoproteins, including p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1, and are involved in cell growth, differentiation and apoptosis [PUBMED:8848831]. Both CBP and P300 have two copies of the TAZ domain, one in the N-terminal region, the other in the C-terminal region. The TAZ1 domain of CBP and P300 forms a complex with CITED2 (CBP/P300-interacting transactivator with ED-rich tail), inhibiting the activity of the hypoxia inducible factor (HIF-1alpha) and thereby attenuating the cellular response to low tissue oxygen concentration [PUBMED:12778114]. Adaptation to hypoxia is mediated by transactivation of hypoxia-responsive genes by hypoxia-inducible factor-1 (HIF-1) in complex with the CBP and p300 transcriptional coactivators [PUBMED:11959990].

The TAZ domain adopts an all-alpha fold with zinc-binding sites in the loops connecting the helices. The TAZ1 domain in P300 and the TAZ2 (CH3) domain in CBP have each been shown to have four amphipathic helices, organised by three zinc-binding clusters with HCCC-type coordination [PUBMED:11023789, PUBMED:14594809, PUBMED:15641773].

More information about these proteins can be found at Protein of the Month: Zinc Fingers [PUBMED:].

Gene Ontology

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Domain organisation

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  Seed
(22)
Full
(729)
Representative proteomes NCBI
(660)
Meta
(8)
RP15
(164)
RP35
(240)
RP55
(349)
RP75
(456)
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  Seed
(22)
Full
(729)
Representative proteomes NCBI
(660)
Meta
(8)
RP15
(164)
RP35
(240)
RP55
(349)
RP75
(456)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

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Curation and family details

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Seed source: IPR000197
Previous IDs: none
Type: Family
Author: De Guzman R, Mian N, Bateman A
Number in seed: 22
Number in full: 729
Average length of the domain: 76.50 aa
Average identity of full alignment: 38 %
Average coverage of the sequence by the domain: 8.52 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 19.0 19.0
Trusted cut-off 19.0 19.1
Noise cut-off 18.6 18.8
Model length: 75
Family (HMM) version: 11
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Species distribution

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Interactions

There is 1 interaction for this family. More...

HIF-1a_CTAD

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the zf-TAZ domain has been found. There are 16 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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