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    SIR4 chromatin-silencing protein SIR4 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 851813, updated on 18-Sep-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    SIR telomere silencing depends on nuclear envelope lipids and modulates sensitivity to a lysolipid.

    SIR telomere silencing depends on nuclear envelope lipids and modulates sensitivity to a lysolipid.
    Sosa Ponce ML, Remedios MH, Moradi-Fard S, Cobb JA, Zaremberg V., Free PMC Article

    04/14/2023
    Esc1-interacting region of Sir4 is Dbf4-related H-BRCT domain

    Discovery and Evolution of New Domains in Yeast Heterochromatin Factor Sir4 and Its Partner Esc1.
    Faure G, Jézéquel K, Roisné-Hamelin F, Bitard-Feildel T, Lamiable A, Marcand S, Callebaut I., Free PMC Article

    03/23/2019
    A direct interaction between Ubp10 and the Sir2/4 sub-complex facilitates Ubp10 recruitment to chromatin via a co-assembly mechanism.

    Recruitment and allosteric stimulation of a histone-deubiquitinating enzyme during heterochromatin assembly.
    Zukowski A, Al-Afaleq NO, Duncan ED, Yao T, Johnson AM., Free PMC Article

    02/9/2019
    the silencing factor Sir4, NE-associated Esc1, the SUMO E3 ligase Siz2, and the nuclear pore complex (NPC) protein Nup170-physically and functionally interact with one another and a subset of NPC components (nucleoporins or Nups).

    Yeast silencing factor Sir4 and a subset of nucleoporins form a complex distinct from nuclear pore complexes.
    Lapetina DL, Ptak C, Roesner UK, Wozniak RW., Free PMC Article

    10/7/2017
    Repair of UV-induced DNA lesions in Saccharomyces cerevisiae telomeres is moderated by Sir2 and Sir3, and inhibited by yKu-Sir4 interaction.

    Repair of UV-induced DNA lesions in natural Saccharomyces cerevisiae telomeres is moderated by Sir2 and Sir3, and inhibited by yKu-Sir4 interaction.
    Guintini L, Tremblay M, Toussaint M, D'Amours A, Wellinger RE, Wellinger RJ, Conconi A., Free PMC Article

    09/9/2017
    silencing requires Sir2, a highly-conserved NAD(+)-dependent histone deacetylase. At locations other than the rDNA, silencing also requires additional Sir proteins, Sir1, Sir3, and Sir4 that together form a repressive heterochromatin-like structure termed silent chromatin.

    The Nuts and Bolts of Transcriptionally Silent Chromatin in Saccharomyces cerevisiae.
    Gartenberg MR, Smith JS., Free PMC Article

    05/27/2017
    nse3-1/ sir4 Delta double mutants show additive defects for telomere shortening and TPE indicating the contribution of Smc5/6 to telomere homeostasis is only in partial overlap with SIR factor silencing. These findings support a role for Smc5/6 in telomere maintenance that is separate from its canonical role(s) in HR-mediated events during replication and telomere elongation.

    Smc5/6 Is a Telomere-Associated Complex that Regulates Sir4 Binding and TPE.
    Moradi-Fard S, Sarthi J, Tittel-Elmer M, Lalonde M, Cusanelli E, Chartrand P, Cobb JA., Free PMC Article

    05/27/2017
    data support a model whereby the demethylation of histone H3 K79 and changes in Sir4 abundance and availability define two rate-limiting steps that regulate de novo assembly of heterochromatin

    Competition between Heterochromatic Loci Allows the Abundance of the Silencing Protein, Sir4, to Regulate de novo Assembly of Heterochromatin.
    Larin ML, Harding K, Williams EC, Lianga N, Doré C, Pilon S, Langis É, Yanofsky C, Rudner AD., Free PMC Article

    06/4/2016
    The authors show that Sir4 - a previously identified Ku-binding protein that is a component of telomeric silent chromatin - is required for Ku-mediated telomere lengthening and telomerase recruitment.

    The Ku subunit of telomerase binds Sir4 to recruit telomerase to lengthen telomeres in S. cerevisiae.
    Hass EP, Zappulla DC., Free PMC Article

    05/21/2016
    These results demonstrate that the SCF(Dia2) complex is involved in transcriptional silencing, ubiquitylates Sir4, and regulates transcriptional silencing during the cell cycle.

    The SCFDia2 ubiquitin E3 ligase ubiquitylates Sir4 and functions in transcriptional silencing.
    Burgess RJ, Zhou H, Han J, Li Q, Zhang Z., Free PMC Article

    01/5/2013
    Sir4 N-terminus plays two roles in SIR-mediated silencing: it contributes to epigenetic repression by stabilizing the SIR-mediated protection of linker DNA; and, as a target of phosphorylation, it can destabilize silencing in a regulated manner.

    Regulating repression: roles for the sir4 N-terminus in linker DNA protection and stabilization of epigenetic states.
    Kueng S, Tsai-Pflugfelder M, Oppikofer M, Ferreira HC, Roberts E, Tsai C, Roloff TC, Sack R, Gasser SM., Free PMC Article

    09/29/2012
    Elongator mutants influence telomeric gene silencing by impairing efficient expression of SIR4.

    Elongator complex influences telomeric gene silencing and DNA damage response by its role in wobble uridine tRNA modification.
    Chen C, Huang B, Eliasson M, Rydén P, Byström AS., Free PMC Article

    01/14/2012
    Data show that the Rap1 C-terminal domain establishes two parallel inhibitory pathways through the proteins Rif2 and Sir4.

    Multiple pathways inhibit NHEJ at telomeres.
    Marcand S, Pardo B, Gratias A, Cahun S, Callebaut I., Free PMC Article

    01/21/2010
    Sir3-Sir4 complexes form progressively higher order assemblies with increasing protein concentration, with implications for the mechanism of gene silencing.

    Domain structure and protein interactions of the silent information regulator Sir3 revealed by screening a nested deletion library of protein fragments.
    King DA, Hall BE, Iwamoto MA, Win KZ, Chang JF, Ellenberger T.

    01/21/2010
    sir2 and sir4, but not sir3, have roles in silencing of DNA breakage and recombination

    Involvement of Sir2/4 in silencing of DNA breakage and recombination on mouse YACs during yeast meiosis.
    Klieger Y, Yizhar O, Zenvirth D, Shtepel-Milman N, Snoek M, Simchen G., Free PMC Article

    01/21/2010
    Results suggest that the telomeric component Sir4p interact genetically and physically with GSP1 and together they regulate proper telomeric function in yeast.

    The nuclear GTPase Gsp1p can affect proper telomeric function through the Sir4 protein in Saccharomyces cerevisiae.
    Clément M, Deshaies F, de Repentigny L, Belhumeur P.

    01/21/2010
    Sir4(PAD)-mediated tethering requires either the Ku complex or Esc1, an acidic protein that is localized to the inner face of the nuclear envelope even in the absence of Ku, Sir4 or Nup133

    Separation of silencing from perinuclear anchoring functions in yeast Ku80, Sir4 and Esc1 proteins.
    Taddei A, Hediger F, Neumann FR, Bauer C, Gasser SM., Free PMC Article

    01/21/2010
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