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Gene Review

LOC427882  -  histone H1

Gallus gallus

 
 
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Disease relevance of LOC427882

 

High impact information on LOC427882

  • However, by Northern analysis of RNA from several adult chicken tissues, as well as from embryonal skeletal muscle in vivo and in vitro, we have observed histone H1 transcripts longer than those predicted on the basis of the published genomic sequences [5].
  • Polyadenylation and U7 snRNP-mediated cleavage: alternative modes of RNA 3' processing in two avian histone H1 genes [5].
  • During interphase, HMG1 readily diffuses out of nuclei after permeabilization of the nuclear membranes with detergents, whereas histone H1 remains associated to chromatin [6].
  • We have identified a clear preference of histone H1 for CpG-methylated DNA, irrespective of DNA sequence [7].
  • While expression of wild-type p34cdc2 did not interfere with normal cell cycle progression, p34cdc2 carrying mutations at both Thr14 and Tyr15 displayed increased histone H1 kinase activity and rapidly induced premature mitotic events, including chromosome condensation and lamina disassembly [8].
 

Biological context of LOC427882

  • The periodicity of micrococcal nuclease-sensitive sites in the linker regions associated with histone H1 or H5 is 10.4 base pairs, suggesting that the spatial organization of the linker region in the higher-order structure of chromatin is similar to that in isolated nucleosomes [9].
  • A gene-specific promoter element is required for optimal expression of the histone H1 gene in S-phase [10].
  • We have previously reported that a serine(threonine) protein kinase that phosphorylates histone H1 in vitro is activated by tyrosine phosphorylation in v-Src-transformed rat 3Y1 fibroblasts [11].
  • High-affinity binding sites for histone H1 in plasmid DNA [12].
  • These results imply that yeast has a protein or protein domain that serves the role of the histone H 1 found in higher cells; physical and genetic studies of the yeast activity could help elucidate the structure and function of H 1 [13].
 

Anatomical context of LOC427882

  • This type of folding generates a fiber in which the nucleosome-nucleosome contacts established in the zig-zag ribbon are maintained and in which the histone H1 molecules occupy equivalent sites [14].
  • The interaction of histone H1 isolated from chicken erythrocytes with restriction fragments from plasmids pBR322 and pUC19 was studied by gel electrophoresis [12].
  • In SDS/polyacrylamide gels MDBP-2 has an apparent molecular mass of 21 kDa, and antibodies directed against calf thymus total histone H1 cross-react with MDBP-2 [15].
  • These results suggest that myelin basic protein and histone H1, widely used in biochemical characterization studies of the phosphatase, may not be physiological substrates, and that the cytoplasm, microsomes, and synaptoplasm may prove to be useful sources for the identification of physiological substrates [16].
  • Histone H1 variants play individual roles in transcription regulation in the DT40 chicken B cell line [17].
 

Associations of LOC427882 with chemical compounds

  • Polycations such as polylysine, polyarginine, histone H1, histones H2A-H2B, and protamine were observed to induce minimal positive stress [18].
  • Six histone H1 subtypes and histone H5, isolated from chicken erythrocyte nuclei, were visualized on acid/urea polyacrylamide gels [19].
  • The possibility that histone H1 binds preferentially to DNA containing 5-methylcytosine in the dinucleotide CpG is appealing, as it could help to explain the repressive effects of methylation on gene activity [20].
  • PKC activity, measured as 32P incorporation into histone H1 in the presence of calcium (500 microM), phosphatidylserine (100 micrograms/ml), and diolein (3.3 micrograms/ml) minus the incorporation in the presence of calcium alone, was detected in neuronal cytosolic (207 +/- 33 pmol/min/mg) and membrane (33 +/- 8 pmol/min/mg) fractions [21].
  • Existing methods for the analysis of histone H1 by capillary electrophoresis (CE) employ acidic buffers (pH <3.0) to suppress silanol ionization and minimize the loss of these extremely basic proteins by adsorption to capillary walls [22].
 

Other interactions of LOC427882

 

Analytical, diagnostic and therapeutic context of LOC427882

References

  1. Association of the human papillomavirus type 11 E1 protein with histone H1. Swindle, C.S., Engler, J.A. J. Virol. (1998) [Pubmed]
  2. Deposition of histone H1 onto reconstituted nucleosome arrays inhibits both initiation and elongation of transcripts by T7 RNA polymerase. O'Neill, T.E., Meersseman, G., Pennings, S., Bradbury, E.M. Nucleic Acids Res. (1995) [Pubmed]
  3. The chlamydial EUO gene encodes a histone H1-specific protease. Kaul, R., Hoang, A., Yau, P., Bradbury, E.M., Wenman, W.M. J. Bacteriol. (1997) [Pubmed]
  4. Specificities of IgM and IgG anti-histone H1 autoantibodies in autoimmune mice. Monestier, M., Fasy, T.M., Debbas, M.E., Bohm, L. Clin. Exp. Immunol. (1990) [Pubmed]
  5. Polyadenylation and U7 snRNP-mediated cleavage: alternative modes of RNA 3' processing in two avian histone H1 genes. Kirsh, A.L., Groudine, M., Challoner, P.B. Genes Dev. (1989) [Pubmed]
  6. High mobility group 1 protein is not stably associated with the chromosomes of somatic cells. Falciola, L., Spada, F., Calogero, S., Langst, G., Voit, R., Grummt, I., Bianchi, M.E. J. Cell Biol. (1997) [Pubmed]
  7. A preference of histone H1 for methylated DNA. McArthur, M., Thomas, J.O. EMBO J. (1996) [Pubmed]
  8. Mutations of p34cdc2 phosphorylation sites induce premature mitotic events in HeLa cells: evidence for a double block to p34cdc2 kinase activation in vertebrates. Krek, W., Nigg, E.A. EMBO J. (1991) [Pubmed]
  9. Regulation of the higher-order structure of chromatin by histones H1 and H5. Allan, J., Cowling, G.J., Harborne, N., Cattini, P., Craigie, R., Gould, H. J. Cell Biol. (1981) [Pubmed]
  10. A gene-specific promoter element is required for optimal expression of the histone H1 gene in S-phase. Dalton, S., Wells, J.R. EMBO J. (1988) [Pubmed]
  11. Activation of YRP kinase by v-Src and protein kinase C-mediated signal transduction pathways. Scholz, G., Felder, M.P., Hanafusa, H. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  12. High-affinity binding sites for histone H1 in plasmid DNA. Yaneva, J., Schroth, G.P., van Holde, K.E., Zlatanova, J. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  13. Higher-order structure of Saccharomyces cerevisiae chromatin. Lowary, P.T., Widom, J. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  14. The higher-order structure of chromatin: evidence for a helical ribbon arrangement. Woodcock, C.L., Frado, L.L., Rattner, J.B. J. Cell Biol. (1984) [Pubmed]
  15. The repressor MDBP-2 is a member of the histone H1 family that binds preferentially in vitro and in vivo to methylated nonspecific DNA sequences. Jost, J.P., Hofsteenge, J. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  16. Quantitative subcellular localization of calmodulin-dependent phosphatase in chick forebrain. Anthony, F.A., Winkler, M.A., Edwards, H.H., Cheung, W.Y. J. Neurosci. (1988) [Pubmed]
  17. Histone H1 variants play individual roles in transcription regulation in the DT40 chicken B cell line. Takami, Y., Nishi, R., Nakayama, T. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  18. In vitro studies on the maintenance of transcription-induced stress by histones and polyamines. Peng, H.F., Jackson, V. J. Biol. Chem. (2000) [Pubmed]
  19. Characterization of the six chicken histone H1 proteins and alignment with their respective genes. Shannon, M.F., Wells, J.R. J. Biol. Chem. (1987) [Pubmed]
  20. Binding of histone H1 to DNA is indifferent to methylation at CpG sequences. Campoy, F.J., Meehan, R.R., McKay, S., Nixon, J., Bird, A. J. Biol. Chem. (1995) [Pubmed]
  21. Insulin stimulates the activity of a novel protein kinase C, PKC-epsilon, in cultured fetal chick neurons. Heidenreich, K.A., Toledo, S.P., Brunton, L.L., Watson, M.J., Daniel-Issakani, S., Strulovici, B. J. Biol. Chem. (1990) [Pubmed]
  22. Capillary electrophoresis of histone H1 variants at neutral pH in dynamically modified fused- silica tubing. Mizzen, C.A., McLachlan, D.R. Electrophoresis (2000) [Pubmed]
  23. Differentiation-dependent alterations in histone methylation and chromatin architecture at the inducible chicken lysozyme gene. Lefevre, P., Lacroix, C., Tagoh, H., Hoogenkamp, M., Melnik, S., Ingram, R., Bonifer, C. J. Biol. Chem. (2005) [Pubmed]
  24. Histone H2A ubiquitination does not preclude histone H1 binding, but it facilitates its association with the nucleosome. Jason, L.J., Finn, R.M., Lindsey, G., Ausió, J. J. Biol. Chem. (2005) [Pubmed]
  25. The methylated DNA binding protein-2-H1 (MDBP-2-H1) consists of histone H1 subtypes which are truncated at the C-terminus. Schwarz, S., Hess, D., Jost, J.P. Nucleic Acids Res. (1997) [Pubmed]
  26. Multiple structural features are responsible for the nuclease sensitivity of the active ovalbumin gene. Senear, A.W., Palmiter, R.D. J. Biol. Chem. (1981) [Pubmed]
  27. The characterisation of 1SF monomer nucleosomes from hen oviduct and the partial characterisation of a third HMG14/17-like in such nucleosomes. Goodwin, G.H., Wright, C.A., Johns, E.W. Nucleic Acids Res. (1981) [Pubmed]
  28. Mitosis-specific phosphorylation of p60c-src by p34cdc2-associated protein kinase. Morgan, D.O., Kaplan, J.M., Bishop, J.M., Varmus, H.E. Cell (1989) [Pubmed]
  29. Intracellular distribution of histone mRNAs in human fibroblasts studied by in situ hybridization. Lawrence, J.B., Singer, R.H., Villnave, C.A., Stein, J.L., Stein, G.S. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  30. Amino acid sequence of histone H1 at the ADP-ribose-accepting site and ADP-ribose X histone-H1 adduct as an inhibitor of cyclic-AMP-dependent phosphorylation. Ushiroyama, T., Tanigawa, Y., Tsuchiya, M., Matsuura, R., Ueki, M., Sugimoto, O., Shimoyama, M. Eur. J. Biochem. (1985) [Pubmed]
  31. Modification of the lysine residues of histones H1 and H5: effects on structure and on the binding to chromatin. Jordano, J., Barbero, J.L., Montero, F., Palacián, E. Mol. Biol. Rep. (1985) [Pubmed]
 
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