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Hist1h1e  -  histone cluster 1, H1e

Mus musculus

Synonyms: H1 VAR.2, H1-4, H1.4, H1e, H1f4, ...
 
 
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Disease relevance of Hist1h1e

 

High impact information on Hist1h1e

  • Mammalian somatic cells contain a set of H1 linker-histone subtypes, H1 (0) and H1a to H1e, that bind to nucleosome core particles and to the linker DNA between nucleosomes [3].
  • Mice contain at least seven nonallelic subtypes of H1, including the somatic variants H1a through H1e, the testis-specific variant H1t, and the replacement linker histone H1(0) [4].
  • To further investigate the in vivo role of individual mammalian H1s in development, we generated mice lacking H1c, H1d, or H1e by homologous recombination in mouse embryonic stem cells [5].
  • HP1 binds specifically to Lys26-methylated histone H1.4, whereas simultaneous Ser27 phosphorylation blocks HP1 binding [6].
  • The linker histone H1.4 is methylated on Lys(26) (K26/H1.4), but the role of this methylation in downstream events remains unknown [6].
 

Biological context of Hist1h1e

  • Specific inhibitory effect of H1e histone somatic variant on in vitro DNA-methylation process [7].
  • We found, using this highly purified system, that H1e protein binds preferentially and cooperatively to the GC-rich region of the DNA [8].
 

Anatomical context of Hist1h1e

  • Whole-mount in situ hybridization using cloned H1c and H1e cDNAs revealed that the mRNAs were present in the cytoplasm of oocytes and 1-cell embryos, in contrast to the sea urchin early embryo where they are sequestered in the cell nucleus [9].
  • H1c and H1e from both cell lines show in the quiescent state a relatively high specific activity comparable with that of H1(0) [10].
  • In vivo phosphorylation of the five histone H1 variants H1a-H1e including H1(0) in NIH 3T3 mouse fibroblasts was examined during the cell cycle by using a combination of HPLC techniques and conventional AU gel electrophoresis [2].
 

Associations of Hist1h1e with chemical compounds

 

Other interactions of Hist1h1e

  • Two others, H1d and H1e, are present in a second patch, while the H1b gene is at least 500 kb away in a patch containing 14 core histone genes [12].
  • H1b is much less varied, while H1d and H1e are invariant by these electrophoretic criteria [13].

References

  1. In vitro binding of H1 histone subtypes to nucleosomal organized mouse mammary tumor virus long terminal repeat promotor. Talasz, H., Sapojnikova, N., Helliger, W., Lindner, H., Puschendorf, B. J. Biol. Chem. (1998) [Pubmed]
  2. In vivo phosphorylation of histone H1 variants during the cell cycle. Talasz, H., Helliger, W., Puschendorf, B., Lindner, H. Biochemistry (1996) [Pubmed]
  3. Mammalian linker-histone subtypes differentially affect gene expression in vivo. Alami, R., Fan, Y., Pack, S., Sonbuchner, T.M., Besse, A., Lin, Q., Greally, J.M., Skoultchi, A.I., Bouhassira, E.E. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  4. Mice develop normally without the H1(0) linker histone. Sirotkin, A.M., Edelmann, W., Cheng, G., Klein-Szanto, A., Kucherlapati, R., Skoultchi, A.I. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  5. Individual somatic H1 subtypes are dispensable for mouse development even in mice lacking the H1(0) replacement subtype. Fan, Y., Sirotkin, A., Russell, R.G., Ayala, J., Skoultchi, A.I. Mol. Cell. Biol. (2001) [Pubmed]
  6. HP1 binds specifically to Lys26-methylated histone H1.4, whereas simultaneous Ser27 phosphorylation blocks HP1 binding. Daujat, S., Zeissler, U., Waldmann, T., Happel, N., Schneider, R. J. Biol. Chem. (2005) [Pubmed]
  7. Specific inhibitory effect of H1e histone somatic variant on in vitro DNA-methylation process. Zardo, G., Santoro, R., D'Erme, M., Reale, A., Guidobaldi, L., Caiafa, P., Strom, R. Biochem. Biophys. Res. Commun. (1996) [Pubmed]
  8. Preferential binding of H1e histone to GC-rich DNA. Wellman, S.E., Sittman, D.B., Chaires, J.B. Biochemistry (1994) [Pubmed]
  9. Chromatin modifications during oogenesis in the mouse: removal of somatic subtypes of histone H1 from oocyte chromatin occurs post-natally through a post-transcriptional mechanism. Clarke, H.J., Bustin, M., Oblin, C. J. Cell. Sci. (1997) [Pubmed]
  10. G1- and S-phase synthesis of histone H1 subtypes from mouse NIH fibroblasts and rat C6 glioma cells. Talasz, H., Helliger, W., Puschendorf, B., Lindner, H. Biochemistry (1993) [Pubmed]
  11. Effect of buffer composition on the migration order and separation of histone H1 subtypes. Lindner, H., Helliger, W., Sarg, B., Meraner, C. Electrophoresis (1995) [Pubmed]
  12. The mouse histone H1 genes: gene organization and differential regulation. Wang, Z.F., Sirotkin, A.M., Buchold, G.M., Skoultchi, A.I., Marzluff, W.F. J. Mol. Biol. (1997) [Pubmed]
  13. Differences in evolutionary stability among mammalian H1 subtypes. Implications for the roles of H1 subtypes in chromatin. Lennox, R.W. J. Biol. Chem. (1984) [Pubmed]
 
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