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FUBP1  -  far upstream element (FUSE) binding protein 1

Homo sapiens

 
 
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Disease relevance of FUBP1

 

Psychiatry related information on FUBP1

  • The lowered folate binding capacity of FBP is not explained by a defect of the FBP1 or FBP2 gene, but most likely occurs as a secondary phenomenon in Rett syndrome [5].
 

High impact information on FUBP1

  • FBP bound to FUSE acts through TFIIH at the promoter [6].
  • The KH domains of the FUSE-binding protein (FBP), a regulator of c-myc expression, bind in vivo and in vitro to the single-stranded far-upstream element (FUSE), 1,500 base pairs upstream from the c-myc promoter [6].
  • Deletion and insertion mutagenesis of FBP defined a novel single-strand DNA-binding domain [7].
  • To determine whether the FUSE site, in vivo, possesses single-strand conformation, and therefore could be bound by FBP, cells were treated with potassium permanganate (KMnO4) to modify unpaired bases [7].
  • Transfection of FBP into human leukemia cells stimulated c-myc-promoter-driven expression from a reporter plasmid in a FUSE-dependent manner [7].
 

Biological context of FUBP1

 

Anatomical context of FUBP1

  • Using a strand-displacement assay with 32P labeled oligonucleotide annealed to M13 ssDNA we have purified to apparent homogeneity and characterized a novel DNA unwinding enzyme from HeLa cell nuclei, human DNA helicase V (HDH V) [11].
  • In fibroblasts, the coordinate expression of FBP and c-myc throughout all phases of the cell cycle is consistent with FBP's role as a growth-dependent regulator of c-myc expression [12].
  • In concert with a loss of c-myc expression, both FUSE binding protein (FBP) mRNA and protein levels disappeared in HL60 cells after PMA-induced differentiation, due to a drop in the rate of transcription that was measured by nuclear runoff [12].
  • When T cells and fibroblasts were stimulated to transit from G0 into the cell cycle, there was a dramatic rise of both FBP mRNA and DNA sequence specific nuclear FBP binding activity, which correlated with the appearance of c-myc mRNA [12].
  • All metastatic lymph nodes strongly reacted with FBP [4].
 

Associations of FUBP1 with chemical compounds

  • Upon treatment with the transcription inhibitor actinomycin D, FBP completely re-localized into dots, but did not exit from the nucleus [8].
  • Partial amino acid sequencing revealed that one of the RNA binding proteins coincides with FBP (far upstream element binding protein), previously characterized as a protein that resembles hnRNP K and which binds to a single-stranded, pyrimidine-rich DNA sequence upstream of the c -myc gene to activate its expression [13].
  • Identification of far upstream element-binding protein-1 as an authentic Parkin substrate [2].
  • Glutaraldehyde- or formalin-fixed intact and trypsinized BSF gave results similar to those obtained with living cells and SBA, WGA, and FBP [14].
  • Binding of FBP to the sensor surface could be blocked at concentrations as high as 1 microM with a 100-fold excess of folic acid, indicating the specificity of the folate-FBP interaction and the absence of nonspecific binding to the functionalized surface [15].
 

Physical interactions of FUBP1

 

Co-localisations of FUBP1

 

Other interactions of FUBP1

  • In addition to its transcriptional role, FBP and its closely related siblings FBP2 (KSRP) and FBP3 have been reported to bind RNA and participate in various steps of RNA processing, transport or catabolism [8].
 

Analytical, diagnostic and therapeutic context of FUBP1

  • The M:(r) determined by SDS-PAGE (66 kDa) corresponds to that measured under native conditions, suggesting that HDH V exists as a monomer in the nucleus [16].
  • Gel shift analyses using full length FBP and a related transcription factor confirm that a small-molecule lead compound inhibits DNA binding in a specific manner [17].
  • In this report, we describe the development of a quartz crystal microbalance biosensor for detection of folate binding protein (FBP) [15].
  • The role of the acid/base residue was probed by site-directed mutagenesis and steady-state and pre-steady-state kinetics on a representative member of this family, FBP aldolase [3].
  • Comparison of the fibrin-binding affinities of proteolytic FBPs from the N-terminus (25.9 kDa FBP), the C-terminus (14.4 kDa) and intact Fn by ELISA yielded estimated Kd values of 216, 18 and 2.1 nM, respectively [18].

References

  1. The FUSE/FBP/FIR/TFIIH system is a molecular machine programming a pulse of c-myc expression. Liu, J., Kouzine, F., Nie, Z., Chung, H.J., Elisha-Feil, Z., Weber, A., Zhao, K., Levens, D. EMBO J. (2006) [Pubmed]
  2. Identification of far upstream element-binding protein-1 as an authentic Parkin substrate. Ko, H.S., Kim, S.W., Sriram, S.R., Dawson, V.L., Dawson, T.M. J. Biol. Chem. (2006) [Pubmed]
  3. New superfamily members identified for Schiff-base enzymes based on verification of catalytically essential residues. Choi, K.H., Lai, V., Foster, C.E., Morris, A.J., Tolan, D.R., Allen, K.N. Biochemistry (2006) [Pubmed]
  4. Reactivity to fucose-binding proteins of Lotus tetragonolobus correlates with metastatic phenotype of transitional cell carcinoma of the bladder. Shirahama, T., Ikoma, M., Muramatsu, H., Muramatsu, T., Ohi, Y. J. Urol. (1992) [Pubmed]
  5. Reduced folate transport to the CNS in female Rett patients. Ramaekers, V.T., Hansen, S.I., Holm, J., Opladen, T., Senderek, J., Häusler, M., Heimann, G., Fowler, B., Maiwald, R., Blau, N. Neurology (2003) [Pubmed]
  6. Structure and dynamics of KH domains from FBP bound to single-stranded DNA. Braddock, D.T., Louis, J.M., Baber, J.L., Levens, D., Clore, G.M. Nature (2002) [Pubmed]
  7. A sequence-specific, single-strand binding protein activates the far upstream element of c-myc and defines a new DNA-binding motif. Duncan, R., Bazar, L., Michelotti, G., Tomonaga, T., Krutzsch, H., Avigan, M., Levens, D. Genes Dev. (1994) [Pubmed]
  8. Nuclear targeting determinants of the far upstream element binding protein, a c-myc transcription factor. He, L., Weber, A., Levens, D. Nucleic Acids Res. (2000) [Pubmed]
  9. The FBP interacting repressor targets TFIIH to inhibit activated transcription. Liu, J., He, L., Collins, I., Ge, H., Libutti, D., Li, J., Egly, J.M., Levens, D. Mol. Cell (2000) [Pubmed]
  10. The far upstream element-binding proteins comprise an ancient family of single-strand DNA-binding transactivators. Davis-Smyth, T., Duncan, R.C., Zheng, T., Michelotti, G., Levens, D. J. Biol. Chem. (1996) [Pubmed]
  11. Human DNA helicase V, a novel DNA unwinding enzyme from HeLa cells. Tuteja, N., Rahman, K., Tuteja, R., Falaschi, A. Nucleic Acids Res. (1993) [Pubmed]
  12. A transactivator of c-myc is coordinately regulated with the proto-oncogene during cellular growth. Bazar, L., Harris, V., Sunitha, I., Hartmann, D., Avigan, M. Oncogene (1995) [Pubmed]
  13. Identification of two proteins that bind to a pyrimidine-rich sequence in the 3'-untranslated region of GAP-43 mRNA. Irwin, N., Baekelandt, V., Goritchenko, L., Benowitz, L.I. Nucleic Acids Res. (1997) [Pubmed]
  14. Cell surface saccharides of Trypanosoma lewis i. II. Lectin-mediated agglutination and fine-structure cytochemical detection of lectin-binding sites. Dwyer, D.M. J. Cell. Sci. (1976) [Pubmed]
  15. Detection of folate binding protein with enhanced sensitivity using a functionalized quartz crystal microbalance sensor. Henne, W.A., Doorneweerd, D.D., Lee, J., Low, P.S., Savran, C. Anal. Chem. (2006) [Pubmed]
  16. Identification of human DNA helicase V with the far upstream element-binding protein. Vindigni, A., Ochem, A., Triolo, G., Falaschi, A. Nucleic Acids Res. (2001) [Pubmed]
  17. NMR-driven discovery of benzoylanthranilic acid inhibitors of far upstream element binding protein binding to the human oncogene c-myc promoter. Huth, J.R., Yu, L., Collins, I., Mack, J., Mendoza, R., Isaac, B., Braddock, D.T., Muchmore, S.W., Comess, K.M., Fesik, S.W., Clore, G.M., Levens, D., Hajduk, P.J. J. Med. Chem. (2004) [Pubmed]
  18. Comparison of the fibrin-binding activities in the N- and C-termini of fibronectin. Rostagno, A.A., Schwarzbauer, J.E., Gold, L.I. Biochem. J. (1999) [Pubmed]
 
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