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    ZUO1 zuotin [ Saccharomyces cerevisiae S288C ]

    Gene ID: 853202, updated on 13-Apr-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    The ribosome-associated chaperone Zuo1 controls translation upon TORC1 inhibition.

    The ribosome-associated chaperone Zuo1 controls translation upon TORC1 inhibition.
    Black A, Williams TD, Soubigou F, Joshua IM, Zhou H, Lamoliatte F, Rousseau A., Free PMC Article

    12/21/2023
    Zuo1, a ribosome-associated J protein, is involved in glucose repression in Saccharomyces cerevisiae.

    Zuo1, a ribosome-associated J protein, is involved in glucose repression in Saccharomyces cerevisiae.
    Yamada Y, Shiroma A, Hirai S, Iwasaki J.

    08/25/2023
    Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding.

    Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding.
    Chen Y, Tsai B, Li N, Gao N., Free PMC Article

    07/2/2022
    Pathway of Hsp70 interactions at the ribosome.

    Pathway of Hsp70 interactions at the ribosome.
    Lee K, Ziegelhoffer T, Delewski W, Berger SE, Sabat G, Craig EA., Free PMC Article

    10/23/2021
    Zuo1 supports G4 structure formation and directs repair toward nucleotide excision repair.

    Zuo1 supports G4 structure formation and directs repair toward nucleotide excision repair.
    De Magis A, Götz S, Hajikazemi M, Fekete-Szücs E, Caterino M, Juranek S, Paeschke K., Free PMC Article

    09/26/2020
    Ssz1 is catalytically inert and cannot adopt the closed conformation, but the substrate binding domain beta is completed by Zuo1.

    Structural insights into a unique Hsp70-Hsp40 interaction in the eukaryotic ribosome-associated complex.
    Weyer FA, Gumiero A, Gesé GV, Lapouge K, Sinning I.

    07/8/2017
    This study presents new structural and cross-linking data allowing more precise positioning of Saccharomyces cerevisiae ribosome-associated J protein-Hsp70 chaperone Zuo1 near the 60S polypeptide-exit site and suggesting interactions of Zuo1 with the ribosomal protein eL31 and 25S rRNA helix 24.

    Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits.
    Lee K, Sharma R, Shrestha OK, Bingman CA, Craig EA., Free PMC Article

    05/20/2017
    The yeast ribosome-associated complex is composed of HSP40 (Zuotin) and HSP70 (Ssz1). RAC stabilizes the 80S ribosome in nonrotated, classical conformation.

    Structural basis for interaction of a cotranslational chaperone with the eukaryotic ribosome.
    Zhang Y, Ma C, Yuan Y, Zhu J, Li N, Chen C, Wu S, Yu L, Lei J, Gao N.

    02/21/2015
    Unfolding of Zuo1's C-terminal helical bundle domain results in ribosome dissociation followed by activation of Pdr1 via a direct interaction.

    Unfolding of the C-terminal domain of the J-protein Zuo1 releases autoinhibition and activates Pdr1-dependent transcription.
    Ducett JK, Peterson FC, Hoover LA, Prunuske AJ, Volkman BF, Craig EA., Free PMC Article

    03/9/2013
    study presents structural analyses of the ribosome-associated complex (RAC) consisting (Hsp70) Ssz1 and the Hsp40 Zuo1; a unique alpha-helical domain in Zuo1 mediates ribosome interaction of RAC near the ribosomal proteins L22e and L31e and ribosomal RNA helix H59

    Structural characterization of a eukaryotic chaperone--the ribosome-associated complex.
    Leidig C, Bange G, Kopp J, Amlacher S, Aravind A, Wickles S, Witte G, Hurt E, Beckmann R, Sinning I.

    03/2/2013
    Zuo1 activates Pdr1 causing premature growth arrest of cells during the diauxic shift, through quorum sensing, as they adapt to the changing environmental conditions.

    Role for the molecular chaperones Zuo1 and Ssz1 in quorum sensing via activation of the transcription factor Pdr1.
    Prunuske AJ, Waltner JK, Kuhn P, Gu B, Craig EA., Free PMC Article

    03/17/2012
    Both Jjj1 and Zuo1 associate with nuclear 60S ribosomal biogenesis intermediates and play an important role in nuclear rRNA processing, leading to mature 25S rRNA

    A ribosome-anchored chaperone network that facilitates eukaryotic ribosome biogenesis.
    Albanèse V, Reissmann S, Frydman J., Free PMC Article

    06/28/2010
    structural analysis of teh ribosome-associated complex (RAC) reveals an unusual Hsp70/Hsp40 interaction between zuotin and ssz

    Structural analysis of the ribosome-associated complex (RAC) reveals an unusual Hsp70/Hsp40 interaction.
    Fiaux J, Horst J, Scior A, Preissler S, Koplin A, Bukau B, Deuerling E., Free PMC Article

    03/1/2010
    Zuo1 and Ssz1 together with the Hsp70 homolog Ssb1/2 form a functional triad involved in translation and early polypeptide folding processes.

    Functional characterization of the atypical Hsp70 subunit of yeast ribosome-associated complex.
    Conz C, Otto H, Peisker K, Gautschi M, Wölfle T, Mayer MP, Rospert S.

    01/21/2010
    ssb and zuo1 have a role in cation influx in Saccharomyces cerevisiae membranes

    Broad sensitivity of Saccharomyces cerevisiae lacking ribosome-associated chaperone ssb or zuo1 to cations, including aminoglycosides.
    Kim SY, Craig EA., Free PMC Article

    01/21/2010
    Zuo1 efficiently stimulates the ATPase activity of Ssb only when in complex with another Hsp70, Ssz1.

    The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1.
    Huang P, Gautschi M, Walter W, Rospert S, Craig EA.

    01/21/2010
    A plausible role of the ZUO1 chaperone is to stabilize genetic networks, thus making them more tolerant to malfunctioning of their constituents.

    Why molecular chaperones buffer mutational damage: a case study with a yeast Hsp40/70 system.
    Bobula J, Tomala K, Jez E, Wloch DM, Borts RH, Korona R., Free PMC Article

    01/21/2010
    Jjj1, when overexpressed, is able to partially substitute for the Zuo1:Ssb chaperone machinery by recruiting Ssa to the ribosome, facilitating its interaction with nascent polypeptide chains

    The specialized cytosolic J-protein, Jjj1, functions in 60S ribosomal subunit biogenesis.
    Meyer AE, Hung NJ, Yang P, Johnson AW, Craig EA., Free PMC Article

    01/21/2010
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