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The fidelity of DNA replication, particularly on GC-rich templates, is reduced by defects of the Fe-S cluster in DNA polymerase δ. / Kiktev, Denis A.; Dominska, Margaret; Zhang, Tony; Dahl, Joseph; Stepchenkova, Elena I.; Mieczkowski, Piotr; Burgers, Peter M.; Lujan, Scott; Burkholder, Adam; Kunkel, Thomas A.; Petes, Thomas D.

In: Nucleic Acids Research, Vol. 49, No. 10, 04.06.2021, p. 5623-5636.

Research output: Contribution to journalArticlepeer-review

Harvard

Kiktev, DA, Dominska, M, Zhang, T, Dahl, J, Stepchenkova, EI, Mieczkowski, P, Burgers, PM, Lujan, S, Burkholder, A, Kunkel, TA & Petes, TD 2021, 'The fidelity of DNA replication, particularly on GC-rich templates, is reduced by defects of the Fe-S cluster in DNA polymerase δ', Nucleic Acids Research, vol. 49, no. 10, pp. 5623-5636. https://doi.org/10.1093/nar/gkab371

APA

Kiktev, D. A., Dominska, M., Zhang, T., Dahl, J., Stepchenkova, E. I., Mieczkowski, P., Burgers, P. M., Lujan, S., Burkholder, A., Kunkel, T. A., & Petes, T. D. (2021). The fidelity of DNA replication, particularly on GC-rich templates, is reduced by defects of the Fe-S cluster in DNA polymerase δ. Nucleic Acids Research, 49(10), 5623-5636. https://doi.org/10.1093/nar/gkab371

Vancouver

Author

Kiktev, Denis A. ; Dominska, Margaret ; Zhang, Tony ; Dahl, Joseph ; Stepchenkova, Elena I. ; Mieczkowski, Piotr ; Burgers, Peter M. ; Lujan, Scott ; Burkholder, Adam ; Kunkel, Thomas A. ; Petes, Thomas D. / The fidelity of DNA replication, particularly on GC-rich templates, is reduced by defects of the Fe-S cluster in DNA polymerase δ. In: Nucleic Acids Research. 2021 ; Vol. 49, No. 10. pp. 5623-5636.

BibTeX

@article{712086b997e94111852ce6a5fa492dbd,
title = "The fidelity of DNA replication, particularly on GC-rich templates, is reduced by defects of the Fe-S cluster in DNA polymerase δ",
abstract = "Iron-sulfur clusters (4Fe-4S) exist in many enzymes concerned with DNA replication and repair. The contribution of these clusters to enzymatic activity is not fully understood. We identified the MET18 (MMS19) gene of Saccharomyces cerevisiae as a strong mutator on GC-rich genes. Met18p is required for the efficient insertion of iron-sulfur clusters into various proteins. met18 mutants have an elevated rate of deletions between short flanking repeats, consistent with increased DNA polymerase slippage. This phenotype is very similar to that observed in mutants of POL3 (encoding the catalytic subunit of Pol δ) that weaken binding of the iron-sulfur cluster. Comparable mutants of POL2 (Pol {\"I}μ) do not elevate deletions. Further support for the conclusion that met18 strains result in impaired DNA synthesis by Pol δare the observations that Pol δisolated from met18 strains has less bound iron and is less processive in vitro than the wild-type holoenzyme. ",
keywords = "Catalytic Domain, DNA Polymerase III/metabolism, DNA Repair, DNA Replication, DNA-Directed DNA Polymerase/metabolism, Iron-Sulfur Proteins/metabolism, Protein Binding, Saccharomyces cerevisiae Proteins/metabolism, Saccharomyces cerevisiae/genetics, Transcription Factors/metabolism, MUTATION-RATE, MICROSATELLITE, MISMATCH REPAIR, SACCHAROMYCES-CEREVISIAE, BASE, GENE, GENOME-WIDE ANALYSIS, DELETIONS, DOMAINS, SUBUNIT",
author = "Kiktev, {Denis A.} and Margaret Dominska and Tony Zhang and Joseph Dahl and Stepchenkova, {Elena I.} and Piotr Mieczkowski and Burgers, {Peter M.} and Scott Lujan and Adam Burkholder and Kunkel, {Thomas A.} and Petes, {Thomas D.}",
note = "Publisher Copyright: {\textcopyright} 2021 The Author(s). Published by Oxford University Press on behalf of Nucleic Acids Research.",
year = "2021",
month = jun,
day = "4",
doi = "10.1093/nar/gkab371",
language = "English",
volume = "49",
pages = "5623--5636",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "10",

}

RIS

TY - JOUR

T1 - The fidelity of DNA replication, particularly on GC-rich templates, is reduced by defects of the Fe-S cluster in DNA polymerase δ

AU - Kiktev, Denis A.

AU - Dominska, Margaret

AU - Zhang, Tony

AU - Dahl, Joseph

AU - Stepchenkova, Elena I.

AU - Mieczkowski, Piotr

AU - Burgers, Peter M.

AU - Lujan, Scott

AU - Burkholder, Adam

AU - Kunkel, Thomas A.

AU - Petes, Thomas D.

N1 - Publisher Copyright: © 2021 The Author(s). Published by Oxford University Press on behalf of Nucleic Acids Research.

PY - 2021/6/4

Y1 - 2021/6/4

N2 - Iron-sulfur clusters (4Fe-4S) exist in many enzymes concerned with DNA replication and repair. The contribution of these clusters to enzymatic activity is not fully understood. We identified the MET18 (MMS19) gene of Saccharomyces cerevisiae as a strong mutator on GC-rich genes. Met18p is required for the efficient insertion of iron-sulfur clusters into various proteins. met18 mutants have an elevated rate of deletions between short flanking repeats, consistent with increased DNA polymerase slippage. This phenotype is very similar to that observed in mutants of POL3 (encoding the catalytic subunit of Pol δ) that weaken binding of the iron-sulfur cluster. Comparable mutants of POL2 (Pol Ïμ) do not elevate deletions. Further support for the conclusion that met18 strains result in impaired DNA synthesis by Pol δare the observations that Pol δisolated from met18 strains has less bound iron and is less processive in vitro than the wild-type holoenzyme.

AB - Iron-sulfur clusters (4Fe-4S) exist in many enzymes concerned with DNA replication and repair. The contribution of these clusters to enzymatic activity is not fully understood. We identified the MET18 (MMS19) gene of Saccharomyces cerevisiae as a strong mutator on GC-rich genes. Met18p is required for the efficient insertion of iron-sulfur clusters into various proteins. met18 mutants have an elevated rate of deletions between short flanking repeats, consistent with increased DNA polymerase slippage. This phenotype is very similar to that observed in mutants of POL3 (encoding the catalytic subunit of Pol δ) that weaken binding of the iron-sulfur cluster. Comparable mutants of POL2 (Pol Ïμ) do not elevate deletions. Further support for the conclusion that met18 strains result in impaired DNA synthesis by Pol δare the observations that Pol δisolated from met18 strains has less bound iron and is less processive in vitro than the wild-type holoenzyme.

KW - Catalytic Domain

KW - DNA Polymerase III/metabolism

KW - DNA Repair

KW - DNA Replication

KW - DNA-Directed DNA Polymerase/metabolism

KW - Iron-Sulfur Proteins/metabolism

KW - Protein Binding

KW - Saccharomyces cerevisiae Proteins/metabolism

KW - Saccharomyces cerevisiae/genetics

KW - Transcription Factors/metabolism

KW - MUTATION-RATE

KW - MICROSATELLITE

KW - MISMATCH REPAIR

KW - SACCHAROMYCES-CEREVISIAE

KW - BASE

KW - GENE

KW - GENOME-WIDE ANALYSIS

KW - DELETIONS

KW - DOMAINS

KW - SUBUNIT

UR - http://www.scopus.com/inward/record.url?scp=85108124225&partnerID=8YFLogxK

U2 - 10.1093/nar/gkab371

DO - 10.1093/nar/gkab371

M3 - Article

C2 - 34019669

AN - SCOPUS:85108124225

VL - 49

SP - 5623

EP - 5636

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 10

ER -

ID: 88539255