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Nucleic Acids Research, 2003, Vol. 31, No. 10 2475-2482
© 2003 Oxford University Press

The histone 3 lysine 36 methyltransferase, SET2, is involved in transcriptional elongation

Daniel Schaft, Assen Roguev, Kimberly M. Kotovic1, Anna Shevchenko1, Mihail Sarov, Andrej Shevchenko1, Karla M. Neugebauer1 and A. Francis Stewart

BIOTEC, Technische Universitaet Dresden, c/o MPI-CBG, Pfotenhauerstrasse 108, D-01307, Germany and 1 Max Planck Institute for Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, D-01307, Germany

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors

Existing evidence indicates that SET2, the histone 3 lysine 36 methyltransferase of Saccharomyces cerevisiae, is a transcriptional repressor. Here we show by five main lines of evidence that SET2 is involved in transcriptional elongation. First, most, if not all, subunits of the RNAP II holoenzyme co-purify with SET2. Second, all of the co-purifying RNAP II subunit, RPO21, was phosphorylated at serines 5 and 2 of the C-terminal domain (CTD) tail, indicating that the SET2 association is specific to either the elongating or SSN3 repressed forms (or both) of RNAP II. Third, the association of SET2 with CTD phosphorylated RPO21 remained in the absence of ssn3. Fourth, in the absence of ssn3, mRNA production from gal1 required SET2. Fifth, SET2 was detected on gal1 by in vivo crosslinking after, but not before, the induction of transcription. Similarly, SET2 physically associated with the transcribed region of pdr5 but was not detected on gal1 or pdr5 promoter regions. Since SET2 is also a histone methyltransferase, these results suggest a role for histone 3 lysine 36 methylation in transcriptional elongation.


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