This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ren, Q.
Right arrow Articles by Gorovsky, M. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ren, Q.
Right arrow Articles by Gorovsky, M. A.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, April 2003, p. 2778-2789, Vol. 23, No. 8
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.8.2778-2789.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

The Nonessential H2A N-Terminal Tail Can Function as an Essential Charge Patch on the H2A.Z Variant N-Terminal Tail

Qinghu Ren{dagger} and Martin A. Gorovsky*

Department of Biology, University of Rochester, Rochester, New York 14627

Received 2 October 2002/ Returned for modification 19 November 2002/ Accepted 21 January 2003

Tetrahymena thermophila cells contain three forms of H2A: major H2A.1 and H2A.2, which make up ~80% of total H2A, and a conserved variant, H2A.Z. We showed previously that acetylation of H2A.Z was essential (Q. Ren and M. A. Gorovsky, Mol. Cell 7:1329-1335, 2001). Here we used in vitro mutagenesis of lysine residues, coupled with gene replacement, to identify the sites of acetylation of the N-terminal tail of the major H2A and to analyze its function in vivo. Tetrahymena cells survived with all five acetylatable lysines replaced by arginines plus a mutation that abolished acetylation of the N-terminal serine normally found in the wild-type protein. Thus, neither posttranslational nor cotranslational acetylation of major H2A is essential. Surprisingly, the nonacetylatable N-terminal tail of the major H2A was able to replace the essential function of the acetylation of the H2A.Z N-terminal tail. Tail-swapping experiments between H2A.1 and H2A.Z revealed that the nonessential acetylation of the major H2A N-terminal tail can be made to function as an essential charge patch in place of the H2A.Z N-terminal tail and that while the pattern of acetylation of an H2A N-terminal tail is determined by the tail sequence, the effects of acetylation on viability are determined by properties of the H2A core and not those of the N-terminal tail itself.

* Corresponding author. Mailing address: Department of Biology, University of Rochester, Rochester, NY 14627. Phone: (585) 275-6988. Fax: (585) 275-2070. E-mail: goro{at}mail.rochester.edu.

{dagger} Present address: The Institute for Genomic Research, Rockville, MD 20850.

Molecular and Cellular Biology, April 2003, p. 2778-2789, Vol. 23, No. 8
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.8.2778-2789.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Wu, N., Yue, H.-M., Chen, B., Gui, J.-F. (2009). Histone H2A Has a Novel Variant in Fish Oocytes. Biol. Reprod. 81: 275-283 [Abstract] [Full Text]  
  • Polevoda, B., Hoskins, J., Sherman, F. (2009). Properties of Nat4, an N{alpha}-Acetyltransferase of Saccharomyces cerevisiae That Modifies N Termini of Histones H2A and H4. Mol. Cell. Biol. 29: 2913-2924 [Abstract] [Full Text]  
  • Song, X., Gjoneska, E., Ren, Q., Taverna, S. D., Allis, C. D., Gorovsky, M. A. (2007). Phosphorylation of the SQ H2A.X Motif Is Required for Proper Meiosis and Mitosis in Tetrahymena thermophila. Mol. Cell. Biol. 27: 2648-2660 [Abstract] [Full Text]  
  • Thambirajah, A. A., Dryhurst, D., Ishibashi, T., Li, A., Maffey, A. H., Ausio, J. (2006). H2A.Z Stabilizes Chromatin in a Way That Is Dependent on Core Histone Acetylation. J. Biol. Chem. 281: 20036-20044 [Abstract] [Full Text]  
  • Babiarz, J. E., Halley, J. E., Rine, J. (2006). Telomeric heterochromatin boundaries require NuA4-dependent acetylation of histone variant H2A.Z in Saccharomy cescerevisiae.. Genes Dev. 20: 700-710 [Abstract] [Full Text]  
  • Kamakaka, R. T., Biggins, S. (2005). Histone variants: deviants?. Genes Dev. 19: 295-316 [Abstract] [Full Text]  
  • Krogan, N. J., Baetz, K., Keogh, M.-C., Datta, N., Sawa, C., Kwok, T. C. Y., Thompson, N. J., Davey, M. G., Pootoolal, J., Hughes, T. R., Emili, A., Buratowski, S., Hieter, P., Greenblatt, J. F. (2004). Regulation of chromosome stability by the histone H2A variant Htz1, the Swr1 chromatin remodeling complex, and the histone acetyltransferase NuA4. Proc. Natl. Acad. Sci. USA 101: 13513-13518 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»