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    RAD30 DNA-directed DNA polymerase eta [ Saccharomyces cerevisiae S288C ]

    Gene ID: 852028, updated on 14-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Post-translational Regulation of DNA Polymerase eta, a Connection to Damage-Induced Cohesion in Saccharomyces cerevisiae.

    Post-translational Regulation of DNA Polymerase η, a Connection to Damage-Induced Cohesion in Saccharomyces cerevisiae.
    Wu PS, Enervald E, Joelsson A, Palmberg C, Rutishauser D, Hällberg BM, Ström L., Free PMC Article

    07/17/2021
    The interaction between ubiquitin and yeast polymerase eta C terminus does not require the UBZ domain.

    The interaction between ubiquitin and yeast polymerase η C terminus does not require the UBZ domain.
    Duong PTM, Bui ATN, Kim SO, Park HS, Seo YS, Choi BS.

    04/17/2021
    Bypass of DNA interstrand crosslinks by a Rev1-DNA polymerase zeta complex.

    Bypass of DNA interstrand crosslinks by a Rev1-DNA polymerase ζ complex.
    Bezalel-Buch R, Cheun YK, Roy U, Schärer OD, Burgers PM., Free PMC Article

    10/24/2020
    Here we show that the translesion synthesis DNA polymerase eta (Pol eta) plays a role in DNA replication under low deoxyribonucleotides condition triggered by hydroxyurea. In particular, the catalytic reaction performed by Pol eta is detrimental for RNase H deficient cells, causing DNA damage checkpoint activation and G2/M arrest

    RNase H activities counteract a toxic effect of Polymerase η in cells replicating with depleted dNTP pools.
    Meroni A, Nava GM, Bianco E, Grasso L, Galati E, Bosio MC, Delmastro D, Muzi-Falconi M, Lazzaro F., Free PMC Article

    11/30/2019
    Lsm12 is a novel regulator mediating Poleta deubiquitination that regulates its recruitment in response to DNA damage induced by oxidative stress.

    Lsm12 Mediates Deubiquitination of DNA Polymerase η To Help Saccharomyces cerevisiae Resist Oxidative Stress.
    Yao R, Shi L, Wu C, Qiao W, Liu L, Wu J., Free PMC Article

    11/16/2019
    these findings provide insight into the physiological role of DNA synthesis by pol eta and have implications for our understanding of how our genome is replicated to avoid mutagenesis, genome instability and cancer

    DNA polymerase η contributes to genome-wide lagging strand synthesis.
    Kreisel K, Engqvist MKM, Kalm J, Thompson LJ, Boström M, Navarrete C, McDonald JP, Larsson E, Woodgate R, Clausen AR., Free PMC Article

    10/19/2019
    Profiles of base-substitutions created by Polzeta & Poleta of Saccharomyces cerevisiae were analyzed. Poleta created deletions at the lesion in more than 50% of the TLS products, but the formation of the deletions was suppressed by the presence of Polzeta. Polzeta & Poleta cooperatively facilitated the TLS reaction over an abasic site in vitro, suggesting that these two polymerases can cooperate in efficient and high f...

    NGS-based analysis of base-substitution signatures created by yeast DNA polymerase eta and zeta on undamaged and abasic DNA templates in vitro.
    Chen Y, Sugiyama T., Free PMC Article

    12/2/2017
    This study provides further understanding of the mutation mechanism of alkylated lesion for yeast DNA polymerase eta.

    Kinetic analysis of bypass of O(6)- methylguanine by the catalytic core of yeast DNA polymerase eta.
    Liu B, Xue Q, Gu S, Wang W, Chen J, Li Y, Wang C, Zhang H.

    04/29/2017
    These data indicate that under certain conditions, pol eta can compete with the cell's replicases and gain access to undamaged genomic DNA.

    Unlocking the steric gate of DNA polymerase η leads to increased genomic instability in Saccharomyces cerevisiae.
    Donigan KA, Cerritelli SM, McDonald JP, Vaisman A, Crouch RJ, Woodgate R., Free PMC Article

    06/28/2016
    The stability of Pol eta, but not its mRNA level, is cell cycle stage dependent. The half-life of the polymerase is more than fourfold shorter in G1-arrested cells than in those at G2/M.

    The steady-state level and stability of TLS polymerase eta are cell cycle dependent in the yeast S. cerevisiae.
    Plachta M, Halas A, McIntyre J, Sledziewska-Gojska E.

    02/13/2016
    This study provides further understanding in the mutation mechanism of abasic sites for yeast DNA polymerase eta

    Kinetic analysis of bypass of abasic site by the catalytic core of yeast DNA polymerase eta.
    Yang J, Wang R, Liu B, Xue Q, Zhong M, Zeng H, Zhang H.

    11/28/2015
    study found both Pol zeta and Pol eta are necessary for efficient gap repair and that each functions independently of the other; these polymerases may be involved either in initiation of DNA synthesis from the invading end or in a gap-filling process that is required to complete recombination

    Roles of exonucleases and translesion synthesis DNA polymerases during mitotic gap repair in yeast.
    Guo X, Jinks-Robertson S., Free PMC Article

    07/19/2014
    For base pair substitutions, polymerase eta appears to be related in function and epistatic to DNA polymerase zeta which, however, plays the opposite role in the nucleus.

    Role of polymerase η in mitochondrial mutagenesis of Saccharomyces cerevisiae.
    Chatterjee N, Pabla R, Siede W.

    08/31/2013
    our results suggest that other elements in the RAD30 C-terminal region may contribute to the ubiquitin binding in conjunction with the ubiquitin binding zinc finger domain

    A novel ubiquitin binding mode in the S. cerevisiae translesion synthesis DNA polymerase η.
    Ai Y, Wang J, Johnson RE, Haracska L, Prakash L, Zhuang Z., Free PMC Article

    09/10/2011
    exchange of Saccharomyces cerevisiae Poldelta with Poleta requires both the stalling of the holoenzyme and the monoubiquitination of proliferating cell nuclear antigen

    Regulation of polymerase exchange between Poleta and Poldelta by monoubiquitination of PCNA and the movement of DNA polymerase holoenzyme.
    Zhuang Z, Johnson RE, Haracska L, Prakash L, Prakash S, Benkovic SJ., Free PMC Article

    01/21/2010
    Evolutionary conservation of efficient T[CPD]T bypass by HsPoleta and AtPoleta may reflect a high degree of exposure of human skin and plants to solar UV-B radiation

    Biochemical evolution of DNA polymerase eta: properties of plant, human, and yeast proteins.
    Hoffman PD, Curtis MJ, Iwai S, Hays JB.

    01/21/2010
    Data suggest that mutations in the C2H2 motif have no perceptible effect on UV sensitivity or UV mutagenesis, whereas a mutation of the D570 residue adversely affects DNA polymerase eta function.

    Mutations in the ubiquitin binding UBZ motif of DNA polymerase eta do not impair its function in translesion synthesis during replication.
    Acharya N, Brahma A, Haracska L, Prakash L, Prakash S., Free PMC Article

    01/21/2010
    Although in yeast a stable Rev1-Pol eta complex can be formed, this complex formation involves the polymerase-associated domain of Rev1 and not the Rev1 C terminus as in humans.

    Complex formation of yeast Rev1 with DNA polymerase eta.
    Acharya N, Haracska L, Prakash S, Prakash L., Free PMC Article

    01/21/2010
    We show that Pol eta is less accurate than other yeast DNA polym and the accessory proteins have little effect on fidelity when bypassing a TT dimer. Accessory proteins participate in pol eta functions, but they do not suppress UV mutagenesis.

    Effects of accessory proteins on the bypass of a cis-syn thymine-thymine dimer by Saccharomyces cerevisiae DNA polymerase eta.
    McCulloch SD, Wood A, Garg P, Burgers PM, Kunkel TA., Free PMC Article

    01/21/2010
    RAD30 (polymerase eta) replicates through 8-oxoG without any barriers introduced by the presence of the lesion.

    Mechanism of efficient and accurate nucleotide incorporation opposite 7,8-dihydro-8-oxoguanine by Saccharomyces cerevisiae DNA polymerase eta.
    Carlson KD, Washington MT., Free PMC Article

    01/21/2010
    A ubiquitin-binding domain provides enhanced affinity for the ubiquitylated form of PCNA and is essential for in vivo function of the polymerase eta.

    Contributions of ubiquitin- and PCNA-binding domains to the activity of Polymerase eta in Saccharomyces cerevisiae.
    Parker JL, Bielen AB, Dikic I, Ulrich HD., Free PMC Article

    01/21/2010
    These results are the first indication of a role for controlled proteasomal degradation in modulating cellular level of translesion DNA polymerase (Rad30)in eukaryotes.

    Polymerase eta is a short-lived, proteasomally degraded protein that is temporarily stabilized following UV irradiation in Saccharomyces cerevisiae.
    Skoneczna A, McIntyre J, Skoneczny M, Policinska Z, Sledziewska-Gojska E.

    01/21/2010
    Although pol eta could accommodate large bulges and continue synthesis without obstruction, bulge structures in the template, but not in the primer, caused termination of the T7 DNA replication complex

    Ability of polymerase eta and T7 DNA polymerase to bypass bulge structures.
    Cannistraro VJ, Taylor JS.

    01/21/2010
    DNA polymerase eta, which is encoded by the RAD30 gene, is solely responsible for the bypass of T-T dimers but is rarely involved in the bypass of T-T (6-4) photoadducts or abasic sites.

    The relative roles in vivo of Saccharomyces cerevisiae Pol eta, Pol zeta, Rev1 protein and Pol32 in the bypass and mutation induction of an abasic site, T-T (6-4) photoadduct and T-T cis-syn cyclobutane dimer.
    Gibbs PE, McDonald J, Woodgate R, Lawrence CW., Free PMC Article

    01/21/2010
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