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BNC1  -  basonuclin 1

Homo sapiens

Synonyms: BNC, BSN1, HsT19447, Zinc finger protein basonuclin-1
 
 
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Disease relevance of BNC1

  • Gli proteins up-regulate the expression of basonuclin in Basal cell carcinoma [1].
  • FA concentration explained 60, 39, 39, 52 and 71% of the variance of MNed BNC, NPB, BUD, APO and NEC, respectively compared with breast cancer status which only explained 6 and 7% of the variance of MNed BNC and NEC(Two way ANOVA, P<0.0001) [2].
 

High impact information on BNC1

 

Biological context of BNC1

 

Anatomical context of BNC1

  • Association of basonuclin with ability of keratinocytes to multiply and with absence of terminal differentiation [4].
  • In hair follicles, the largest reservoir of basonuclin-containing cells is the outer root sheath, which contains precursors of differentiated cells of the hair shaft and of the epidermis [4].
  • Transfer of the cells to culture medium without supporting 3T3 cells results in a predominantly cytoplasmic concentration of the basonuclin [9].
  • In mouse and rat epidermis, although clusters of basonuclin may be seen in some basal cell nuclei, the protein is mainly concentrated in the cytoplasm [9].
  • Using a transgenic-RNAi approach, we knocked down basonuclin specifically in mouse oocytes, which led to female sub-fertility [10].
 

Associations of BNC1 with chemical compounds

  • Tetraethylammonium block of the BNC1 channel [11].
  • Identification, purification, and characterization of iminodiacetate oxidase from the EDTA-degrading bacterium BNC1 [5].
  • In cultured keratinocytes, the disappearance of basonuclin mRNA is associated with loss of colony-forming ability and the appearance of mRNA for involucrin, a protein characteristic of terminal differentiation [4].
  • These results show that nuclear localization of basonuclin depends on serine dephosphorylation, primarily of Ser-541 [8].
  • A nearly complete basonuclin transiently expressed in cultured keratinocytes localizes predominantly in the nucleus, but substitution of aspartic acid for Ser-541 promotes cytoplasmic localization [8].
 

Other interactions of BNC1

  • The brain Na+ channel-1 (BNC1, also known as MDEG1 or ASIC2) is a member of the DEG/ENaC cation channel family [11].
  • The Ki-67 protein, a nuclear marker for any stage of the multiplication cycle is present in only a subclass of basonuclin-containing cells [4].
  • Near the C-terminal end of basonuclin and on the surface of a putative alpha-helix, there is a stripe of serine residues similar to that of the transcription factor PRDII-BF1 [12].
  • By the method of RNase protection, the 5' ends of the basonuclin mRNA were mapped to four sites distributed over 400 bases of the genomic sequence, a result implying four different basonuclin transcripts within the cell [13].
  • Basonuclin deficiency in oocytes perturbed both RNA polymerase I- and II-mediated transcription, and oocyte morphology was affected (as evidenced by cytoplasmic and cell surface abnormalities) [10].
 

Analytical, diagnostic and therapeutic context of BNC1

  • Moreover, three distinct affinity-purified peptide antibodies gave this unusual pattern of basonuclin antibody staining, which was confirmed by cell fractionation studies [3].
  • Using the evolutionarily highly conserved N-terminal pair of zinc fingers in an electrophoresis mobility shift assay, we demonstrate that the DNA target sequences of basonuclin on the acrocentric chromosomes are likely to be within the promoter region of the 45S rRNA gene transcription unit [14].
  • Neither micronucleus frequency (MN/BNC at 2 Gy) nor proliferating fraction (%BNC at 0 Gy) estimated in vitro (in primary culture) were related to radiotherapy outcome [15].
  • A split BNC connecter was used to allow simultaneous digitisation of analogue output from the ECG receiver unit by a computerised data acquisition system (Po-Ne-Mah) and MiniDisc player (MZ-N710, Sony) [16].
  • When WIL2-NS cells were exposed to neutrophils stimulated with phorbol 12-myristate acetate (PMA) for 1 h, the frequencies of MNed BNC in WIL2-NS cells increased in a dose-dependent manner (30-fold increase at 100 nM PMA) and with an increasing neutrophil:WIL2-NS co-culture ratio [17].

References

  1. Gli proteins up-regulate the expression of basonuclin in Basal cell carcinoma. Cui, C., Elsam, T., Tian, Q., Seykora, J.T., Grachtchouk, M., Dlugosz, A., Tseng, H. Cancer Res. (2004) [Pubmed]
  2. A comparison of folic acid deficiency-induced genomic instability in lymphocytes of breast cancer patients and normal non-cancer controls from a Chinese population in Yunnan. Wang, X., Wu, X., Liang, Z., Huang, Y., Fenech, M., Xue, J. Mutagenesis (2006) [Pubmed]
  3. An unexpected localization of basonuclin in the centrosome, mitochondria, and acrosome of developing spermatids. Yang, Z., Gallicano, G.I., Yu, Q.C., Fuchs, E. J. Cell Biol. (1997) [Pubmed]
  4. Association of basonuclin with ability of keratinocytes to multiply and with absence of terminal differentiation. Tseng, H., Green, H. J. Cell Biol. (1994) [Pubmed]
  5. Identification, purification, and characterization of iminodiacetate oxidase from the EDTA-degrading bacterium BNC1. Liu, Y., Louie, T.M., Payne, J., Bohuslavek, J., Bolton, H., Xun, L. Appl. Environ. Microbiol. (2001) [Pubmed]
  6. Study of the catalytic behavior of montmorillonite/iron(III) and Mn(III) cationic porphyrins. Machado, A.M., Wypych, F., Drechsel, S.M., Nakagaki, S. Journal of colloid and interface science. (2002) [Pubmed]
  7. Basonuclin, a zinc finger protein of keratinocytes and reproductive germ cells, binds to the rRNA gene promoter. Iuchi, S., Green, H. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  8. Nuclear localization of basonuclin in human keratinocytes and the role of phosphorylation. Iuchi, S., Green, H. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  9. Alternative subcellular locations of keratinocyte basonuclin. Iuchi, S., Easley, K., Matsuzaki, K., Weiner, L., O'Connor, N., Green, H. Exp. Dermatol. (2000) [Pubmed]
  10. Basonuclin: a novel mammalian maternal-effect gene. Ma, J., Zeng, F., Schultz, R.M., Tseng, H. Development (2006) [Pubmed]
  11. Tetraethylammonium block of the BNC1 channel. Adams, C.M., Price, M.P., Snyder, P.M., Welsh, M.J. Biophys. J. (1999) [Pubmed]
  12. Basonuclin: a keratinocyte protein with multiple paired zinc fingers. Tseng, H., Green, H. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  13. A GC-rich sequence within the 5' untranslated region of human basonuclin mRNA inhibits its translation. Tang, W., Tseng, H. Gene (1999) [Pubmed]
  14. Basonuclin is associated with the ribosomal RNA genes on human keratinocyte mitotic chromosomes. Tseng, H., Biegel, J.A., Brown, R.S. J. Cell. Sci. (1999) [Pubmed]
  15. Micronucleus assay in vivo provides significant prognostic information in human cervical carcinoma; the updated analysis. Widel, M., Kolosza, Z., Jedruś, S., Lukaszczyk, B., Raczek-Zwierzycka, K., Swierniak, A. Int. J. Radiat. Biol. (2001) [Pubmed]
  16. Recording of ECG signals on a portable MiniDisc recorder for time and frequency domain heart rate variability analysis. Norman, S.E., Eager, R.A., Waran, N.K., Jeffery, L., Schroter, R.C., Marlin, D.J. Physiol. Behav. (2005) [Pubmed]
  17. Cytokinesis-block micronucleus assay in WIL2-NS cells: a sensitive system to detect chromosomal damage induced by reactive oxygen species and activated human neutrophils. Umegaki, K., Fenech, M. Mutagenesis (2000) [Pubmed]
 
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