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Nucleic Acids Research Advance Access published online on September 23, 2009
Nucleic Acids Research, doi:10.1093/nar/gkp765
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© The Author(s) 2009. Published by Oxford University Press.
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Gene Regulation, Chromatin and Epigenetics

Two Dot1 isoforms in Saccharomyces cerevisiae as a result of leaky scanning by the ribosome

Floor Frederiks1, Guus J. J. E. Heynen1, Sjoerd J. van Deventer2, Hans Janssen2 and Fred van Leeuwen1,*

1Division of Gene Regulation and 2Division of Cell Biology II, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands

*To whom correspondence should be addressed. Tel: +31 20 5121973; Fax: +31 20 5121989; Email: Fred.v.leeuwen{at}nki.nl

Received April 3, 2009. Revised August 31, 2009. Accepted September 1, 2009.

Dot1 is a conserved histone methyltransferase that methylates histone H3 on lysine 79. We previously observed that in Saccharomyces cerevisiae, a single DOT1 gene encodes two Dot1 protein species. Here, we show that the relative abundance of the two isoforms changed under nutrient-limiting conditions. A mutagenesis approach showed that the two Dot1 isoforms are produced from two alternative translation start sites as a result of leaky scanning by the ribosome. The leaky scanning was not affected by the 5'- or 3'-untranslated regions of DOT1, indicating that translation initiation is determined by the DOT1 coding sequence. Construction of yeast strains expressing either one of the isoforms showed that both were sufficient for Dot1’s role in global H3K79 methylation and telomeric gene silencing. However, the absence of the long isoform of Dot1 altered the resistance of yeast cells to the chitin-binding drug Calcofluor White, suggesting that the two Dot1 isoforms have a differential function in cell wall biogenesis.


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