Previous Article | Next Article 
Molecular and Cellular Biology, January 2000, p. 61-69, Vol. 20, No. 1
0270-7306/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Histone H1 Is Dispensable for
Methylation-Associated Gene Silencing in Ascobolus immersus
and Essential for Long Life Span
Jose L.
Barra,
Laïla
Rhounim,
Jean-Luc
Rossignol, and
Godeleine
Faugeron*
Institut Jacques Monod, UMR 7592, CNRS/Université Paris 7/Université Paris 6, 75251 Paris
Cedex 05, France
Received 27 July 1999/Returned for modification 13 September
1999/Accepted 28 September 1999
A gene encoding a protein that shows sequence similarity with the
histone H1 family only was cloned in Ascobolus immersus. The deduced peptide sequence presents the characteristic three-domain structure of metazoan linker histones, with a central globular region,
an N-terminal tail, and a long positively charged C-terminal tail. By
constructing an artificial duplication of this gene, named
H1, it was possible to methylate and silence it by the MIP (methylation induced premeiotically) process. This resulted in the
complete loss of the Ascobolus H1 histone. Mutant strains lacking H1 displayed normal methylation-associated gene silencing, underwent MIP, and showed the same methylation-associated chromatin modifications as did wild-type strains. However, they displayed an
increased accessibility of micrococcal nuclease to chromatin, whether
DNA was methylated or not, and exhibited a hypermethylation of the
methylated genome compartment. These features are taken to imply that
Ascobolus H1 histone is a ubiquitous component of chromatin
which plays no role in methylation-associated gene silencing. Mutant
strains lacking histone H1 reproduced normally through sexual crosses
and displayed normal early vegetative growth. However, between 6 and 13 days after germination, they abruptly and consistently stopped growing,
indicating that Ascobolus H1 histone is necessary for long
life span. This constitutes the first observation of a physiologically
important phenotype associated with the loss of H1.
*
Corresponding author. Mailing address: Institut Jacques
Monod, Tour 43, 2 place Jussieu, 75251 Paris Cedex 05, France. Phone: (33) 1 44 27 82 11. Fax: (33) 1 44 27 82 10. E-mail:
faugeron{at}ijm.jussieu.fr.

Present address: Departamento de Química
Biológica, CIQUIBIC-CONICET, Facultad de Ciencias
Químicas, UNC, Ciudad Universitaria,
5000 Córdoba,
Argentina.

Present address: Faculté des Sciences et Techniques,
Mohammèdia,
Morocco.
Molecular and Cellular Biology, January 2000, p. 61-69, Vol. 20, No. 1
0270-7306/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
This article has been cited by other articles:
-
Trojer, P., Zhang, J., Yonezawa, M., Schmidt, A., Zheng, H., Jenuwein, T., Reinberg, D.
(2009). Dynamic Histone H1 Isotype 4 Methylation and Demethylation by Histone Lysine Methyltransferase G9a/KMT1C and the Jumonji Domain-containing JMJD2/KDM4 Proteins. J. Biol. Chem.
284: 8395-8405
[Abstract]
[Full Text]
-
Kim, K., Choi, J., Heo, K., Kim, H., Levens, D., Kohno, K., Johnson, E. M., Brock, H. W., An, W.
(2008). Isolation and Characterization of a Novel H1.2 Complex That Acts as a Repressor of p53-mediated Transcription. J. Biol. Chem.
283: 9113-9126
[Abstract]
[Full Text]
-
Godde, J. S., Ura, K.
(2008). Cracking the Enigmatic Linker Histone Code. J Biochem
143: 287-293
[Abstract]
[Full Text]
-
Ni, J.-Q., Liu, L.-P., Hess, D., Rietdorf, J., Sun, F.-L.
(2006). Drosophila ribosomal proteins are associated with linker histone H1 and suppress gene transcription. Genes Dev.
20: 1959-1973
[Abstract]
[Full Text]
-
Wierzbicki, A. T., Jerzmanowski, A.
(2005). Suppression of Histone H1 Genes in Arabidopsis Results in Heritable Developmental Defects and Stochastic Changes in DNA Methylation. Genetics
169: 997-1008
[Abstract]
[Full Text]
-
Chen, D., Dundr, M., Wang, C., Leung, A., Lamond, A., Misteli, T., Huang, S.
(2005). Condensed mitotic chromatin is accessible to transcription factors and chromatin structural proteins. JCB
168: 41-54
[Abstract]
[Full Text]
-
Dorigo, B., Schalch, T., Kulangara, A., Duda, S., Schroeder, R. R., Richmond, T. J.
(2004). Nucleosome Arrays Reveal the Two-Start Organization of the Chromatin Fiber. Science
306: 1571-1573
[Abstract]
[Full Text]
-
Lin, Q., Inselman, A., Han, X., Xu, H., Zhang, W., Handel, M. A., Skoultchi, A. I.
(2004). Reductions in Linker Histone Levels Are Tolerated in Developing Spermatocytes but Cause Changes in Specific Gene Expression. J. Biol. Chem.
279: 23525-23535
[Abstract]
[Full Text]
-
Borkovich, K. A., Alex, L. A., Yarden, O., Freitag, M., Turner, G. E., Read, N. D., Seiler, S., Bell-Pedersen, D., Paietta, J., Plesofsky, N., Plamann, M., Goodrich-Tanrikulu, M., Schulte, U., Mannhaupt, G., Nargang, F. E., Radford, A., Selitrennikoff, C., Galagan, J. E., Dunlap, J. C., Loros, J. J., Catcheside, D., Inoue, H., Aramayo, R., Polymenis, M., Selker, E. U., Sachs, M. S., Marzluf, G. A., Paulsen, I., Davis, R., Ebbole, D. J., Zelter, A., Kalkman, E. R., O'Rourke, R., Bowring, F., Yeadon, J., Ishii, C., Suzuki, K., Sakai, W., Pratt, R.
(2004). Lessons from the Genome Sequence of Neurospora crassa: Tracing the Path from Genomic Blueprint to Multicellular Organism. Microbiol. Mol. Biol. Rev.
68: 1-108
[Abstract]
[Full Text]
-
Fan, Y., Nikitina, T., Morin-Kensicki, E. M., Zhao, J., Magnuson, T. R., Woodcock, C. L., Skoultchi, A. I.
(2003). H1 Linker Histones Are Essential for Mouse Development and Affect Nucleosome Spacing In Vivo. Mol. Cell. Biol.
23: 4559-4572
[Abstract]
[Full Text]
-
Jedrusik, M. A., Schulze, E.
(2003). Telomeric Position Effect Variegation in Saccharomyces cerevisiae by Caenorhabditis elegans Linker Histones Suggests a Mechanistic Connection between Germ Line and Telomeric Silencing. Mol. Cell. Biol.
23: 3681-3691
[Abstract]
[Full Text]
-
Folco, H. D., Freitag, M., Ramon, A., Temporini, E. D., Alvarez, M. E., Garcia, I., Scazzocchio, C., Selker, E. U., Rosa, A. L.
(2003). Histone H1 Is Required for Proper Regulation of Pyruvate Decarboxylase Gene Expression in Neurosporacrassa. Eukaryot Cell
2: 341-350
[Abstract]
[Full Text]
-
Dou, Y., Bowen, J., Liu, Y., Gorovsky, M. A.
(2002). Phosphorylation and an ATP-dependent process increase the dynamic exchange of H1 in chromatin. JCB
158: 1161-1170
[Abstract]
[Full Text]
-
Jedrusik, M. A., Vogt, S., Claus, P., Schulze, E.
(2002). A novel linker histone-like protein is associated with cytoplasmic filaments in Caenorhabditis elegans. J. Cell Sci.
115: 2881-2891
[Abstract]
[Full Text]
-
Freidkin, I., Katcoff, D. J.
(2001). Specific distribution of the Saccharomyces cerevisiae linker histone homolog HHO1p in the chromatin. Nucleic Acids Res
29: 4043-4051
[Abstract]
[Full Text]
-
KASINSKY, H. E., LEWIS, J. D., DACKS, J. B., AUSIO, J.
(2001). Origin of H1 linker histones. FASEB J.
15: 34-42
[Abstract]
[Full Text]
-
Hellauer, K., Sirard, E., Turcotte, B.
(2001). Decreased Expression of Specific Genes in Yeast Cells Lacking Histone H1. J. Biol. Chem.
276: 13587-13592
[Abstract]
[Full Text]
-
Scrittori, L., Hans, F., Angelov, D., Charra, M., Prigent, C., Dimitrov, S.
(2001). pEg2 Aurora-A Kinase, Histone H3 Phosphorylation, and Chromosome Assembly in Xenopus Egg Extract. J. Biol. Chem.
276: 30002-30010
[Abstract]
[Full Text]