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Molecular and Cellular Biology, August 2008, p. 4915-4926, Vol. 28, No. 16
0270-7306/08/$08.00+0     doi:10.1128/MCB.00001-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Roles for Ctk1 and Spt6 in Regulating the Different Methylation States of Histone H3 Lysine 36{triangledown} ,{dagger}

Michael L. Youdell,1,{ddagger} Kelby O. Kizer,2,{ddagger} Elena Kisseleva-Romanova,1,{ddagger} Stephen M. Fuchs,3 Eris Duro,1 Brian D. Strahl,2,3 and Jane Mellor1*

Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom,1 Department of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599-7260,2 Lineberger Comprehensive Cancer Center, University of North Carolina School of Medicine, Chapel Hill, North Carolina3

Received 1 January 2008/ Returned for modification 7 February 2008/ Accepted 27 May 2008

Set2 (KMT3)-dependent methylation (me) of histone H3 at lysine 36 (H3K36) promotes deacetylation of transcribed chromatin and represses cryptic promoters within genes. Although Set2 is the only methyltransferase (KMTase) for H3K36 in yeast, it is not known if Set2 is regulated or whether the different methylation states at H3K36 are functionally distinct. Here we show that the N-terminal 261 residues of Set2 (Set21-261), containing the SET KMTase domain, are sufficient for H3K36me2, histone deacetylation, and repression of cryptic promoters at STE11. Set2-catalyzed H3K36me2 does not require either Ctk1-dependent phosphorylation of RNA polymerase II (RNAPII) or the presence of the phospho-C-terminal domain (CTD) interaction (SRI) domain of Set2. This finding is consistent with a known correlation between H3K36me2 and whether a gene is on or off, but not the level of activity of a gene. By contrast, H3K36me3 requires Spt6, proline 38 on histone H3 (H3P38), the CTD of RNAPII, Ctk1, and the C-terminal SRI domain of Set2. We suggest that the C-terminal region of Set2, in conjunction with the phosphorylated CTD of RNAPII, influences the KMTase activity to promote H3K36me3 during transcription elongation.

* Corresponding author. Mailing address: Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom. Phone: 44 1865 275303. Fax: 44 1865 275297. E-mail: jane.mellor{at}bioch.ox.ac.uk

{triangledown} Published ahead of print on 9 June 2008.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.

{ddagger} M.L.Y., K.O.K., and E.K.-R. made an equal contribution to this work.

Molecular and Cellular Biology, August 2008, p. 4915-4926, Vol. 28, No. 16
0270-7306/08/$08.00+0     doi:10.1128/MCB.00001-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Egloff, S., Al-Rawaf, H., O'Reilly, D., Murphy, S. (2009). Chromatin Structure Is Implicated in "Late" Elongation Checkpoints on the U2 snRNA and {beta}-Actin Genes. Mol. Cell. Biol. 29: 4002-4013 [Abstract] [Full Text]  
  • Li, B., Jackson, J., Simon, M. D., Fleharty, B., Gogol, M., Seidel, C., Workman, J. L., Shilatifard, A. (2009). Histone H3 Lysine 36 Dimethylation (H3K36me2) Is Sufficient to Recruit the Rpd3s Histone Deacetylase Complex and to Repress Spurious Transcription. J. Biol. Chem. 284: 7970-7976 [Abstract] [Full Text]  
  • Yoh, S. M., Lucas, J. S., Jones, K. A. (2008). The Iws1:Spt6:CTD complex controls cotranscriptional mRNA biosynthesis and HYPB/Setd2-mediated histone H3K36 methylation. Genes Dev. 22: 3422-3434 [Abstract] [Full Text]  


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