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MBC in Press, published online ahead of print October 11, 2006
Mol. Biol. Cell 10.1091/mbc.E06-08-0669

A more recent version of this article appeared on December 1, 2006
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Submitted on August 3, 2006
Revised on September 21, 2006
Accepted on September 29, 2006

Bypassing the Catalytic Activity of SIR2 for SIR Protein Spreading in Saccharomyces cerevisiae

Bo Yang and Ann L. Kirchmaier

Department of Biochemistry and Purdue Cancer Center, Purdue University, West Lafayette, IN 47907

Monitoring Editor: Kerry Bloom

Sir protein spreading along chromosomes and silencing in S. cerevisiae requires the NAD+-dependent histone deacetylase activity of Sir2p. We tested whether this requirement could be bypassed at the HM loci and telomeres in cells containing a stably expressed, but catalytically inactive mutant of Sir2p, sir2-345p, plus histone mutants that mimic the hypoacetylated state normally created by Sir2p. Sir protein spreading was rescued in sir2-345 mutants expressing histones in which key lysine residues in their N termini had been mutated to arginine. Mating in these mutants was also partially restored upon overexpression of Sir3p. Together, these results indicate that histone hypoacetylation is sufficient for Sir protein spreading in the absence of production of 2'-O-acetyl-ADP ribose by sir2p and Sir2p’s enzymatic function for silencing can be bypassed in a subset of cells in a given population. These results also provide genetic evidence for the existence of additional critical substrates of Sir2p for silencing in vivo.

Address correspondence to: Ann L. Kirchmaier (kirchmaier{at}purdue.edu)




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