The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

HIST1H3E  -  histone cluster 1, H3e

Homo sapiens

Synonyms: H3.1, H3/d, H3FD
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

High impact information on HIST1H3E

  • Deposition of the major histone H3 (H3.1) is coupled to DNA synthesis during DNA replication and possibly DNA repair, whereas histone variant H3.3 serves as the replacement variant for the DNA-synthesis-independent deposition pathway [1].
  • A method for rapid sequencing of intact proteins simultaneously from the N and C termini (1-2 s) with online chromatography is described and applied to the characterization of histone H3.1 posttranslational modifications and the identification of an additional member of the H2A gene family [2].
  • Here, we show that mammalian cell lines can be separated into two different groups based on their expression of H3.1, H3.2, and H3.3 at both mRNA and protein levels [3].
  • During the same time 20% of the methylation label was lost from major variant H3.1 protein and more than 50% from the more highly labeled minor variant H3 [4].
  • The H3.3 genes are essentially only expressed in adult tissue, whereas the H3.1 gene is transcribed just in fetal tissue [5].
 

Biological context of HIST1H3E

  • The amino acid sequence has only 69% identity with human H3.3 histone and 67% identity with the human H3.1 histone [6].
 

Associations of HIST1H3E with chemical compounds

  • Dynamic lysine methylation of histone H3 in alfalfa tissue culture cells was studied by labeling with tritiated methionine, purification of variants H3.1 and H3.2 by reversed-phase high pressure liquid chromatography and amino acid analysis [4].
  • In actively growing suspension cultures treated with dactinomycin half-lives of 2 and 7 h were observed for H3.1 and H3.2 mRNAs, respectively. mRNA stabilities were also measured indirectly by histone protein synthesis [7].

References

  1. Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis. Tagami, H., Ray-Gallet, D., Almouzni, G., Nakatani, Y. Cell (2004) [Pubmed]
  2. Protein identification using sequential ion/ion reactions and tandem mass spectrometry. Coon, J.J., Ueberheide, B., Syka, J.E., Dryhurst, D.D., Ausio, J., Shabanowitz, J., Hunt, D.F. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  3. Expression patterns and post-translational modifications associated with mammalian histone H3 variants. Hake, S.B., Garcia, B.A., Duncan, E.M., Kauer, M., Dellaire, G., Shabanowitz, J., Bazett-Jones, D.P., Allis, C.D., Hunt, D.F. J. Biol. Chem. (2006) [Pubmed]
  4. Dynamic methylation of alfalfa histone H3. Waterborg, J.H. J. Biol. Chem. (1993) [Pubmed]
  5. Differential expression of human replacement and cell cycle dependent H3 histone genes. Frank, D., Doenecke, D., Albig, W. Gene (2003) [Pubmed]
  6. Pathogenic Entamoeba histolytica: cDNA cloning of a histone H3 with a divergent primary structure. Födinger, M., Ortner, S., Plaimauer, B., Wiedermann, G., Scheiner, O., Duchêne, M. Mol. Biochem. Parasitol. (1993) [Pubmed]
  7. Histone H3 transcript stability in alfalfa. Kapros, T., Robertson, A.J., Waterborg, J.H. Plant Mol. Biol. (1995) [Pubmed]
 
WikiGenes - Universities