| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 281, Issue 1, 559-568, January 6, 2006
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
1
12||3
From the
Laboratory of Chromatin Biology, The Rockefeller University, New York, New York 10021, the Departments of Chemistry and ||Pathology, University of Virginia, Charlottesville, Virginia 22901, and the ¶Programme in Cell Biology, Research Institute, The Hospital for Sick Children, Toronto, Ontario M5S 1X8, Canada
Covalent histone modifications and the incorporation of histone variants bring about changes in chromatin structure that in turn alter gene expression. Interest in non-allelic histone variants has been renewed, in part because of recent work on H3 (and other) histone variants. However, only in mammals do three non-centromeric H3 variants (H3.1, H3.2, and H3.3) exist. 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. Additionally, the ratio of these variants changes slightly during neuronal differentiation of murine ES cells. This difference in H3 variant expression between cell lines could not be explained by changes in growth rate, cell cycle stages, or chromosomal ploidy, but rather suggests other possibilities, such as changes in H3 variant incorporation during differentiation and tissue- or species-specific H3 variant expression. Moreover, quantitative mass spectrometry analysis of human H3.1, H3.2, and H3.3 showed modification differences between these three H3 variants, suggesting that they may have different biological functions. Specifically, H3.3 contains marks associated with transcriptionally active chromatin, whereas H3.2, in contrast, contains mostly silencing modifications that have been associated with facultative heterochromatin. Interestingly, H3.1 is enriched in both active and repressive marks, although the latter marks are different from those observed in H3.2. Although the biological significance as to why mammalian cells differentially employ three highly similar H3 variants remains unclear, our results underscore potential functional differences between them and reinforce the general view that H3.1 and H3.2 in mammalian cells should not be treated as equivalent proteins.
Received for publication, August 22, 2005 , and in revised form, October 31, 2005.
* This work was supported by Grants GM 40922 (to C. D. A.) and GM 37537 (to D. F. H.) from the National Institutes of Health and from The Rockefeller University Women & Science Fellowship Program (to S. B. H.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
The on-line version of this article (available at http://www.jbc.org) contains supplemental materials, Figs. 1-3, and Tables 1-3.
1 These authors contributed equally to the work.
2 To whom correspondence may be addressed: The Rockefeller University, Box 78, 1230 York Ave., New York, NY 10021. Tel.: 212-327-7839; Fax: 212-327-7849; E-mail: alliscd{at}rockefeller.edu. 3 To whom correspondence may be addressed: University of Virginia, Charlottesville, VA 22908. Tel.: 434-924-3610; Fax: 434-982-2781; E-mail: dfh{at}virginia.edu.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  A. Galvani, R. Courbeyrette, M. Agez, F. Ochsenbein, C. Mann, and J.-Y. Thuret In Vivo Study of the Nucleosome Assembly Functions of ASF1 Histone Chaperones in Human Cells Mol. Cell. Biol., June 1, 2008; 28(11): 3672 - 3685. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. R. Wisniewski, A. Zougman, and M. Mann N{varepsilon}-Formylation of lysine is a widespread post-translational modification of nuclear proteins occurring at residues involved in regulation of chromatin function Nucleic Acids Res., February 2, 2008; 36(2): 570 - 577. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. Mosch, M. Morawski, A. Mittag, D. Lenz, A. Tarnok, and T. Arendt Aneuploidy and DNA Replication in the Normal Human Brain and Alzheimer's Disease J. Neurosci., June 27, 2007; 27(26): 6859 - 6867. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. Jin and G. Felsenfeld Nucleosome stability mediated by histone variants H3.3 and H2A.Z Genes & Dev., June 15, 2007; 21(12): 1519 - 1529. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Y. Takayama and K. Takahashi Differential regulation of repeated histone genes during the fission yeast cell cycle Nucleic Acids Res., May 11, 2007; 35(10): 3223 - 3237. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. Zhang, W. Chen, and P. D. Adams Molecular Dissection of Formation of Senescence-Associated Heterochromatin Foci Mol. Cell. Biol., March 15, 2007; 27(6): 2343 - 2358. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. A. Morris, B. Rao, B. A. Garcia, S. B. Hake, R. L. Diaz, J. Shabanowitz, D. F. Hunt, C. D. Allis, J. D. Lieb, and B. D. Strahl Identification of Histone H3 Lysine 36 Acetylation as a Highly Conserved Histone Modification J. Biol. Chem., March 9, 2007; 282(10): 7632 - 7640. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
B. A. Garcia, S. B. Hake, R. L. Diaz, M. Kauer, S. A. Morris, J. Recht, J. Shabanowitz, N. Mishra, B. D. Strahl, C. D. Allis, et al. Organismal Differences in Post-translational Modifications in Histones H3 and H4 J. Biol. Chem., March 9, 2007; 282(10): 7641 - 7655. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. D. Taverna, B. M. Ueberheide, Y. Liu, A. J. Tackett, R. L. Diaz, J. Shabanowitz, B. T. Chait, D. F. Hunt, and C. D. Allis Long-distance combinatorial linkage between methylation and acetylation on histone H3 N termini PNAS, February 13, 2007; 104(7): 2086 - 2091. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. Zhang, S.-t. Liu, W. Chen, M. Bonner, J. Pehrson, T. J. Yen, and P. D. Adams HP1 Proteins Are Essential for a Dynamic Nuclear Response That Rescues the Function of Perturbed Heterochromatin in Primary Human Cells Mol. Cell. Biol., February 1, 2007; 27(3): 949 - 962. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. R. Wisniewski, A. Zougman, S. Kruger, and M. Mann Mass Spectrometric Mapping of Linker Histone H1 Variants Reveals Multiple Acetylations, Methylations, and Phosphorylation as Well as Differences between Cell Culture and Tissue Mol. Cell. Proteomics, January 1, 2007; 6(1): 72 - 87. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. Kimura, N. Takizawa, E. Allemand, T. Hori, F. J. Iborra, N. Nozaki, M. Muraki, M. Hagiwara, A. R. Krainer, T. Fukagawa, et al. A novel histone exchange factor, protein phosphatase 2C{gamma}, mediates the exchange and dephosphorylation of H2A-H2B J. Cell Biol., November 6, 2006; 175(3): 389 - 400. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Y. Li, G. D. Kao, B. A. Garcia, J. Shabanowitz, D. F. Hunt, J. Qin, C. Phelan, and M. A. Lazar A novel histone deacetylase pathway regulates mitosis by modulating Aurora B kinase activity Genes & Dev., September 15, 2006; 20(18): 2566 - 2579. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. R. Green, H. Yoon, and J. M. Boss Epigenetic Regulation during B Cell Differentiation Controls CIITA Promoter Accessibility J. Immunol., September 15, 2006; 177(6): 3865 - 3873. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
B. A. Garcia, S. Joshi, C. E. Thomas, R. K. Chitta, R. L. Diaz, S. A. Busby, P. C. Andrews, R. R. Ogorzalek Loo, J. Shabanowitz, N. L. Kelleher, et al. Comprehensive Phosphoprotein Analysis of Linker Histone H1 from Tetrahymena thermophila Mol. Cell. Proteomics, September 1, 2006; 5(9): 1593 - 1609. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Y. J. Lee, R. H. Rice, and Y. M. Lee Proteome Analysis of Human Hair Shaft: From Protein Identification to Posttranslational Modification Mol. Cell. Proteomics, May 1, 2006; 5(5): 789 - 800. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. B. Hake and C. D. Allis Inaugural Article: Histone H3 variants and their potential role in indexing mammalian genomes: The "H3 barcode hypothesis" PNAS, April 25, 2006; 103(17): 6428 - 6435. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
