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HIST1H2B8  -  histone cluster 1, H2B-VIII

Gallus gallus

Synonyms: H2B-VIII, HIST1H2BO
 
 
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High impact information on LOC427886

  • The nucleotide sequence homology among the genes within their coding sequences appears to exceed that required for the corresponding protein sequences, suggesting that histone H2B mRNA sequence and structure are both selected during evolution [1].
  • A fragment of 291 bp from the 5' flanking region including 34 bp of the first exon shows promoter activity when introduced upstream of a chicken histone H2B gene and injected into the nuclei of Xenopus laevis oocytes [2].
  • To test for gene elements required for muscle cell specific expression, DNA sequences containing the 5'-flanking regions of the chicken alpha-skeletal actin, beta-cytoplasmic actin, and the histone H2b genes were linked to the coding sequences of the chloramphenicol acetyltransferase gene and transfected into myogenic and non-myogenic cells [3].
  • We have reported earlier the occurrence of a specific histone H2B variant in human testis and sperm [4].
  • Histone H2B is deacetylated more rapidly than H3 and H4 in chicken immature erythrocytes [5].
 

Biological context of LOC427886

 

Anatomical context of LOC427886

  • In the late stage testis chromatin (nucleohistone), ubiquitinated histone H2A.Z was not detected, the level of ubiquitinated histone H2B was reduced, and the amount of diubiquitinated histone H2B increased [9].
  • The fraction of bovine thymus and chicken erythrocyte chromatin enriched in transcriptionally active gene sequences was enriched in mono- and polyubiquitinated species of histones H2A, H2B, and H2A.Z, especially in the ubiquitinated forms of histone H2B [10].
  • 5. The activation of bovine brain phosphodiesterase by calmodulin is inhibited by excess bovine uterus calmodulin-binding protein (histone H2B) [7].
 

Associations of LOC427886 with chemical compounds

 

Analytical, diagnostic and therapeutic context of LOC427886

  • No significant difference between the three types of core particles could be demonstrated by electron microscopy, circular dichroism, or immunochemical analysis with antisera to histone H2B, H2A, and H3 [12].
  • The Mab did show strong ELISA reactions with peptides 1-25 of histone H2B and 1-21 of H3, which correspond to sequences known to be located at the surface of nucleosomes [13].

References

  1. Structure and organization of the chicken H2B histone gene family. Grandy, D.K., Dodgson, J.B. Nucleic Acids Res. (1987) [Pubmed]
  2. Nucleotide sequence of the chicken 5-aminolevulinate synthase gene. Maguire, D.J., Day, A.R., Borthwick, I.A., Srivastava, G., Wigley, P.L., May, B.K., Elliott, W.H. Nucleic Acids Res. (1986) [Pubmed]
  3. Tissue restricted and stage specific transcription is maintained within 411 nucleotides flanking the 5' end of the chicken alpha-skeletal actin gene. Grichnik, J.M., Bergsma, D.J., Schwartz, R.J. Nucleic Acids Res. (1986) [Pubmed]
  4. Characterization of nucleosomes consisting of the human testis/sperm-specific histone H2B variant (hTSH2B). Li, A., Maffey, A.H., Abbott, W.D., Conde e Silva, N., Prunell, A., Siino, J., Churikov, D., Zalensky, A.O., Ausió, J. Biochemistry (2005) [Pubmed]
  5. Properties of chicken erythrocyte histone deacetylase associated with the nuclear matrix. Li, W., Chen, H.Y., Davie, J.R. Biochem. J. (1996) [Pubmed]
  6. Independently evolving chicken histone H2B genes: identification of a ubiquitous H2B-specific 5' element. Harvey, R.P., Robins, A.J., Wells, J.R. Nucleic Acids Res. (1982) [Pubmed]
  7. The binding of calmodulin to myelin basic protein and histone H2B. Grand, R.J., Perry, S.V. Biochem. J. (1980) [Pubmed]
  8. Metabolism of histones in avian erythroid cells. Sung, M.T., Harford, J., Bundman, M., Vidalakas, G. Biochemistry (1977) [Pubmed]
  9. Changes in the histone H2A variant H2A.Z and polyubiquitinated histone species in developing trout testis. Nickel, B.E., Roth, S.Y., Cook, R.G., Allis, C.D., Davie, J.R. Biochemistry (1987) [Pubmed]
  10. Ubiquitinated histone H2B is preferentially located in transcriptionally active chromatin. Nickel, B.E., Allis, C.D., Davie, J.R. Biochemistry (1989) [Pubmed]
  11. Proteolytic digestion studies of chromatin core-histone structure. Identification of limit peptides from histone H2B. Böhm, L., Briand, G., Sautière, P., Crane-Robinson, C. Eur. J. Biochem. (1982) [Pubmed]
  12. Immunochemical detection of changes in chromatin subunits induced by histone H4 acetylation. Muller, S., Erard, M., Burggraf, E., Couppez, M., Sautière, P., Champagne, M., Van Regenmortel, M.H. EMBO J. (1982) [Pubmed]
  13. Detection of nucleosome particles in serum and plasma from patients with systemic lupus erythematosus using monoclonal antibody 4H7. Williams, R.C., Malone, C.C., Meyers, C., Decker, P., Muller, S. J. Rheumatol. (2001) [Pubmed]
 
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