Localization of DNA polymerases eta and iota to the replication machinery is tightly co-ordinated in human cells

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Localization of DNA polymerases eta and iota to the replication machinery is tightly co-ordinated in human cells. / Kannouche, Patricia; Fernández de Henestrosa, Antonio R; Coull, Barry et al.
In: EMBO Journal, Vol. 21, No. 22, 03.03.2003, p. 1223-33.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Kannouche, P, Fernández de Henestrosa, AR, Coull, B, Vidal, AE, Gray, C, Zicha, D, Woodgate, R & Lehmann, AR 2003, 'Localization of DNA polymerases eta and iota to the replication machinery is tightly co-ordinated in human cells', EMBO Journal, vol. 21, no. 22, pp. 1223-33. https://doi.org/10.1093/emboj/cdf618

APA

Kannouche, P., Fernández de Henestrosa, A. R., Coull, B., Vidal, A. E., Gray, C., Zicha, D., Woodgate, R., & Lehmann, A. R. (2003). Localization of DNA polymerases eta and iota to the replication machinery is tightly co-ordinated in human cells. EMBO Journal, 21(22), 1223-33. https://doi.org/10.1093/emboj/cdf618

Vancouver

Kannouche P, Fernández de Henestrosa AR, Coull B, Vidal AE, Gray C, Zicha D et al. Localization of DNA polymerases eta and iota to the replication machinery is tightly co-ordinated in human cells. EMBO Journal. 2003 Mar 3;21(22):1223-33. doi: 10.1093/emboj/cdf618

Author

Kannouche, Patricia ; Fernández de Henestrosa, Antonio R ; Coull, Barry et al. / Localization of DNA polymerases eta and iota to the replication machinery is tightly co-ordinated in human cells. In: EMBO Journal. 2003 ; Vol. 21, No. 22. pp. 1223-33.

Bibtex

@article{043c424cc4d24340ac3f72f20da5b0b1,

title = "Localization of DNA polymerases eta and iota to the replication machinery is tightly co-ordinated in human cells",

abstract = "Y-family DNA polymerases can replicate past a variety of damaged bases in vitro but, with the exception of DNA polymerase eta (poleta), which is defective in xeroderma pigmentosum variants, there is little information on the functions of these polymerases in vivo. Here, we show that DNA polymerase iota (poliota), like poleta, associates with the replication machinery and accumulates at stalled replication forks following DNA-damaging treatment. We show that poleta and poliota foci form with identical kinetics and spatial distributions, suggesting that localization of these two polymerases is tightly co-ordinated within the nucleus. Furthermore, localization of poliota in replication foci is largely dependent on the presence of poleta. Using several different approaches, we demonstrate that poleta and poliota interact with each other physically and that the C-terminal 224 amino acids of poliota are sufficient for both the interaction with poleta and accumulation in replication foci. Our results provide strong evidence that poleta targets poliota to the replication machinery, where it may play a general role in maintaining genome integrity as well as participating in translesion DNA synthesis.",

keywords = "Animals, Caffeine/metabolism, Cell Line, Cell Nucleus/metabolism, DNA Damage, DNA Replication, DNA-Directed DNA Polymerase/metabolism, Fibroblasts/cytology, Humans, Immunohistochemistry, Models, Genetic, Protein Binding, Recombinant Fusion Proteins/metabolism, Two-Hybrid System Techniques, Ultraviolet Rays, Xeroderma Pigmentosum",

author = "Patricia Kannouche and {Fern{\'a}ndez de Henestrosa}, {Antonio R} and Barry Coull and Vidal, {Antonio E} and Colin Gray and Daniel Zicha and Roger Woodgate and Lehmann, {Alan R}",

year = "2003",

month = mar,

day = "3",

doi = "10.1093/emboj/cdf618",

language = "English",

volume = "21",

pages = "1223--33",

journal = "EMBO Journal",

issn = "0261-4189",

publisher = "Nature Publishing Group",

number = "22",

}

RIS

TY - JOUR

T1 - Localization of DNA polymerases eta and iota to the replication machinery is tightly co-ordinated in human cells

AU - Kannouche, Patricia

AU - Fernández de Henestrosa, Antonio R

AU - Coull, Barry

AU - Vidal, Antonio E

AU - Gray, Colin

AU - Zicha, Daniel

AU - Woodgate, Roger

AU - Lehmann, Alan R

PY - 2003/3/3

Y1 - 2003/3/3

N2 - Y-family DNA polymerases can replicate past a variety of damaged bases in vitro but, with the exception of DNA polymerase eta (poleta), which is defective in xeroderma pigmentosum variants, there is little information on the functions of these polymerases in vivo. Here, we show that DNA polymerase iota (poliota), like poleta, associates with the replication machinery and accumulates at stalled replication forks following DNA-damaging treatment. We show that poleta and poliota foci form with identical kinetics and spatial distributions, suggesting that localization of these two polymerases is tightly co-ordinated within the nucleus. Furthermore, localization of poliota in replication foci is largely dependent on the presence of poleta. Using several different approaches, we demonstrate that poleta and poliota interact with each other physically and that the C-terminal 224 amino acids of poliota are sufficient for both the interaction with poleta and accumulation in replication foci. Our results provide strong evidence that poleta targets poliota to the replication machinery, where it may play a general role in maintaining genome integrity as well as participating in translesion DNA synthesis.

AB - Y-family DNA polymerases can replicate past a variety of damaged bases in vitro but, with the exception of DNA polymerase eta (poleta), which is defective in xeroderma pigmentosum variants, there is little information on the functions of these polymerases in vivo. Here, we show that DNA polymerase iota (poliota), like poleta, associates with the replication machinery and accumulates at stalled replication forks following DNA-damaging treatment. We show that poleta and poliota foci form with identical kinetics and spatial distributions, suggesting that localization of these two polymerases is tightly co-ordinated within the nucleus. Furthermore, localization of poliota in replication foci is largely dependent on the presence of poleta. Using several different approaches, we demonstrate that poleta and poliota interact with each other physically and that the C-terminal 224 amino acids of poliota are sufficient for both the interaction with poleta and accumulation in replication foci. Our results provide strong evidence that poleta targets poliota to the replication machinery, where it may play a general role in maintaining genome integrity as well as participating in translesion DNA synthesis.

KW - Animals

KW - Caffeine/metabolism

KW - Cell Line

KW - Cell Nucleus/metabolism

KW - DNA Damage

KW - DNA Replication

KW - DNA-Directed DNA Polymerase/metabolism

KW - Fibroblasts/cytology

KW - Humans

KW - Immunohistochemistry

KW - Models, Genetic

KW - Protein Binding

KW - Recombinant Fusion Proteins/metabolism

KW - Two-Hybrid System Techniques

KW - Ultraviolet Rays

KW - Xeroderma Pigmentosum

U2 - 10.1093/emboj/cdf618

DO - 10.1093/emboj/cdf618

M3 - Journal article

C2 - 12606586

VL - 21

SP - 1223

EP - 1233

JO - EMBO Journal

JF - EMBO Journal

SN - 0261-4189

IS - 22

ER -

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