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Originally published as MBC in Press, 10.1091/mbc.E06-08-0669 on October 11, 2006

Vol. 17, Issue 12, 5287-5297, December 2006

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

Bo Yang, and Ann L. Kirchmaier

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

Submitted August 3, 2006; Revised September 21, 2006; Accepted September 29, 2006
Monitoring Editor: Kerry Bloom

Sir protein spreading along chromosomes and silencing in Saccharomyces 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.

Formula The online version of this contains supplemental material at MBC Online (http://www.molbiolcell.org).

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E06-08-0669) on October 11, 2006.

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

Abbreviations used: SIR, Silent Information Regulator; ChIP, chromatin immunoprecipitation.




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