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THAP1  -  THAP domain containing, apoptosis...

Homo sapiens

 
 
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Disease relevance of THAP1

 

High impact information on THAP1

  • The THAP domain: a novel protein motif with similarity to the DNA-binding domain of P element transposase [2].
  • Together with previous genetic data obtained in C. elegans, our results suggest that cellular THAP proteins may function as zinc-dependent sequence-specific DNA-binding factors with roles in proliferation, apoptosis, cell cycle, chromosome segregation, chromatin modification, and transcriptional regulation [3].
  • In addition, we demonstrate the biochemical function of the THAP domain as a zinc-dependent sequence-specific DNA-binding domain belonging to the zinc-finger superfamily [3].
  • In vitro binding-site selection allowed us to identify an 11-nucleotide consensus DNA-binding sequence specifically recognized by the THAP domain of human THAP1 [3].
  • The four other conserved residues (P, W, F, and P), which define the THAP consensus sequence, were also found to be required for DNA binding [3].
 

Biological context of THAP1

  • Here, we show that THAP1 is a physiologic regulator of EC proliferation and cell-cycle progression, 2 essential processes for angiogenesis [4].
  • The similar phenotypes observed after THAP1 overexpression and silencing suggest that an optimal range of THAP1 expression is essential for EC proliferation [4].
  • Together, these data provide the first links in mammals among THAP proteins, cell proliferation, and pRB/E2F cell-cycle pathways [4].
  • This is the first demonstration of the transcriptional regulatory properties of a human THAP domain protein, and a critical identification of a potential transducer of the repressive signal of hypoacetylated histone H4 in higher eukaryotes [5].
  • We show that the use of 2',4',6'-trihydroxyacetophenone (THAP) as MALDI matrix allows analysis of cross-linked peptide-RNA oligonucleotides in the reflectron mode at high resolution, enabling sufficient accuracy to assign unambiguously cross-linked RNA sequences [6].
 

Anatomical context of THAP1

 

Associations of THAP1 with chemical compounds

  • Negative-ion spectra of pure mono-, di-, and trisialylated oligosaccharides were acquired with either 6-aza-2-thiothymine or 2',4',6'-trihydroxyacetophenone (THAP) in the linear mode [8].
  • In addition, THAP offered improved sensitivity for detection of acidic glycopeptides over alpha-cyano-4-hydroxycinnamic acid [8].
  • Incorporation of ammonium citrate into the matrix, along with vacuum drying of the sample, was required in order to obtain maximum sensitivity with THAP [8].
  • We show that use of the salt-tolerant matrix 2,4,6-trihydroxyacetophenone containing diammonium citrate (THAP/DAC) as an alternative to alpha-cyanohydroxycinnamic acid (HCCA) reduces the need for extensive washing of ZipTip-bound peptides or additional on-target sample clean-up steps [9].
  • We demonstrated the utility of using the THAP/DAC MALDI matrix for peptide sequencing with DNA polymerase beta tryptic peptide mixture, as well as tryptic peptides derived from Xiphophorus maculatus brain extract proteins previously separated by two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) [9].
  • The combination of the mutagenesis and NMR data allowed the mapping of the DNA binding interface of the THAP zinc finger to a highly positively charged area harboring multiple lysine and arginine residues [10].
 

Other interactions of THAP1

  • Retroviral-mediated gene transfer of THAP1 into primary human ECs inhibited proliferation, and large-scale expression profiling with microarrays revealed that THAP1-mediated growth inhibition is due to coordinated repression of pRB/E2F cell-cycle target genes [4].

References

  1. Mutations in THAP1 (DYT6) in early-onset dystonia: a genetic screening study. Bressman, S.B., Raymond, D., Fuchs, T., Heiman, G.A., Ozelius, L.J., Saunders-Pullman, R. Lancet. Neurol (2009) [Pubmed]
  2. The THAP domain: a novel protein motif with similarity to the DNA-binding domain of P element transposase. Roussigne, M., Kossida, S., Lavigne, A.C., Clouaire, T., Ecochard, V., Glories, A., Amalric, F., Girard, J.P. Trends Biochem. Sci. (2003) [Pubmed]
  3. The THAP domain of THAP1 is a large C2CH module with zinc-dependent sequence-specific DNA-binding activity. Clouaire, T., Roussigne, M., Ecochard, V., Mathe, C., Amalric, F., Girard, J.P. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  4. The THAP-zinc finger protein THAP1 regulates endothelial cell proliferation through modulation of pRB/E2F cell-cycle target genes. Cayrol, C., Lacroix, C., Mathe, C., Ecochard, V., Ceribelli, M., Loreau, E., Lazar, V., Dessen, P., Mantovani, R., Aguilar, L., Girard, J.P. Blood (2007) [Pubmed]
  5. Human THAP7 is a chromatin-associated, histone tail-binding protein that represses transcription via recruitment of HDAC3 and nuclear hormone receptor corepressor. Macfarlan, T., Kutney, S., Altman, B., Montross, R., Yu, J., Chakravarti, D. J. Biol. Chem. (2005) [Pubmed]
  6. Complete MALDI-ToF MS analysis of cross-linked peptide-RNA oligonucleotides derived from nonlabeled UV-irradiated ribonucleoprotein particles. Kühn-Hölsken, E., Lenz, C., Sander, B., Lührmann, R., Urlaub, H. RNA (2005) [Pubmed]
  7. THAP1 is a nuclear proapoptotic factor that links prostate-apoptosis-response-4 (Par-4) to PML nuclear bodies. Roussigne, M., Cayrol, C., Clouaire, T., Amalric, F., Girard, J.P. Oncogene (2003) [Pubmed]
  8. Analysis of acidic oligosaccharides and glycopeptides by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Papac, D.I., Wong, A., Jones, A.J. Anal. Chem. (1996) [Pubmed]
  9. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry of 4-sulfophenyl isothiocyanate-derivatized peptides on AnchorChip sample supports using the sodium-tolerant matrix 2,4,6-trihydroxyacetophenone and diammonium citrate. Oehlers, L.P., Perez, A.N., Walter, R.B. Rapid Commun. Mass Spectrom. (2005) [Pubmed]
  10. Structure-function analysis of the THAP zinc finger of THAP1, a large C2CH DNA-binding module linked to Rb/E2F pathways. Bessière, D., Lacroix, C., Campagne, S., Ecochard, V., Guillet, V., Mourey, L., Lopez, F., Czaplicki, J., Demange, P., Milon, A., Girard, J.P., Gervais, V. J. Biol. Chem. (2008) [Pubmed]
 
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