title: Acetylation of the SUN protein Mps3 by Eco1 regulates its function in nuclear organization.
abstract: The Saccharomyces cerevisiae SUN-domain protein Mps3 is required for duplication of the yeast centrosome-equivalent organelle, the spindle pole body (SPB), and it is involved in multiple aspects of nuclear organization, including telomere tethering and gene silencing at the nuclear membrane, establishment of sister chromatid cohesion, and repair of certain types of persistent DNA double-stranded breaks. How these diverse SUN protein functions are regulated is unknown. Here we show that the Mps3 N-terminus is a substrate for the acetyltransferase Eco1/Ctf7 in vitro and in vivo and map the sites of acetylation to three lysine residues adjacent to the Mps3 transmembrane domain. Mutation of these residues shows that acetylation is not essential for growth, SPB duplication, or distribution in the nuclear membrane. However, analysis of nonacetylatable mps3 mutants shows that this modification is required for accurate sister chromatid cohesion and for chromosome recruitment to the nuclear membrane. Acetylation of Mps3 by Eco1 is one of the few regulatory mechanisms known to control nuclear organization.
authors.affiliation: Stowers Institute for Medical Research, Kansas City, MO 64110, USA.
authors.forename: Suman
authors.initials: S
authors.lastname: Ghosh
authors.forename: Jennifer M
authors.initials: JM
authors.lastname: Gardner
authors.forename: Christine J
authors.initials: CJ
authors.lastname: Smoyer
authors.forename: Jennifer M
authors.initials: JM
authors.lastname: Friederichs
authors.forename: Jay R
authors.initials: JR
authors.lastname: Unruh
authors.forename: Brian D
authors.initials: BD
authors.lastname: Slaughter
authors.forename: Richard
authors.initials: R
authors.lastname: Alexander
authors.forename: Robert D
authors.initials: RD
authors.lastname: Chisholm
authors.forename: Kenneth K
authors.initials: KK
authors.lastname: Lee
authors.forename: Jerry L
authors.initials: JL
authors.lastname: Workman
authors.forename: Sue L
authors.initials: SL
authors.lastname: Jaspersen
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D002467:Cell Nucleus / Q000378:metabolism*; D002842:Chromatids / Q000378:metabolism; D004260:DNA Repair; D008239:Lysine / Q000737:chemistry / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008938:Mitosis; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017384:Sequence Deletion; D008941:Spindle Apparatus / Q000378:metabolism; D016615:Telomere / Q000378:metabolism
chemical_list: D008565:Membrane Proteins; C471174:Mps3 protein, S cerevisiae; D009687:Nuclear Proteins; D029701:Saccharomyces cerevisiae Proteins; D000123:Acetyltransferases; C118076:ECO1 protein, S cerevisiae; D008239:Lysine