Nature Genetics32, 378 - 383 (2002)
Published online: 15 October 2002; | doi:10.1038/ng1017
Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine16 and spreading of heterochromatin
Noriyuki Suka, Kunheng Luo
& Michael Grunstein
Department of Biological Chemistry, UCLA School of Medicine and the Molecular Biology Institute, Boyer Hall, University of California, Los Angeles, California 90095, USA.
Correspondence should be addressed to Michael Grunstein mg@mbi.ucla.edu
The Sir3 protein helps form telomeric heterochromatin by interacting with hypoacetylated histone H4 lysine 16 (H4−Lys16). The molecular nature of the heterochromatin boundary is still unknown. Here we show that the MYST-like acetyltransferase Sas2p is required for the acetylation (Ac) of H4−Lys16 in euchromatin. In a sas2 strain or a phenocopy Lys16Arg mutant, Sir3p spreads from roughly 3 kb to roughly 15 kb, causing hypoacetylation and repression of adjacent chromatin. We also found that disruption of Sir3p binding in a deacetylase-deficient Sir 2 strain can be suppressed by sas2. These data indicate that opposing effects of Sir2p and Sas2p on acetylation of H4−Lys16 maintain the boundary at telomeric heterochromatin.
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strain or a phenocopy Lys16Arg mutant, Sir3p spreads from roughly 3 kb to roughly 15 kb, causing hypoacetylation and repression of adjacent chromatin. We also found that disruption of Sir3p binding in a deacetylase-deficient Sir 2
