Dynamics of the Eukaryotic Replicative Helicase at Lagging-Strand Protein Barriers Support the Steric Exclusion Model

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Dynamics of the Eukaryotic Replicative Helicase at Lagging-Strand Protein Barriers Support the Steric Exclusion Model. / Kose, Hazal B.; Larsen, Nicolai B.; Duxin, Julien P.; Yardimci, Hasan.

In: Cell Reports, Vol. 26, No. 8, 2019, p. 2113-2125.e6.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Kose, HB, Larsen, NB, Duxin, JP & Yardimci, H 2019, 'Dynamics of the Eukaryotic Replicative Helicase at Lagging-Strand Protein Barriers Support the Steric Exclusion Model', Cell Reports, vol. 26, no. 8, pp. 2113-2125.e6. https://doi.org/10.1016/j.celrep.2019.01.086

APA

Kose, H. B., Larsen, N. B., Duxin, J. P., & Yardimci, H. (2019). Dynamics of the Eukaryotic Replicative Helicase at Lagging-Strand Protein Barriers Support the Steric Exclusion Model. Cell Reports, 26(8), 2113-2125.e6. https://doi.org/10.1016/j.celrep.2019.01.086

Vancouver

Kose HB, Larsen NB, Duxin JP, Yardimci H. Dynamics of the Eukaryotic Replicative Helicase at Lagging-Strand Protein Barriers Support the Steric Exclusion Model. Cell Reports. 2019;26(8):2113-2125.e6. https://doi.org/10.1016/j.celrep.2019.01.086

Author

Kose, Hazal B. ; Larsen, Nicolai B. ; Duxin, Julien P. ; Yardimci, Hasan. / Dynamics of the Eukaryotic Replicative Helicase at Lagging-Strand Protein Barriers Support the Steric Exclusion Model. In: Cell Reports. 2019 ; Vol. 26, No. 8. pp. 2113-2125.e6.

Bibtex

@article{f3f735ebc7784c97aa5f425eee874ed0,
title = "Dynamics of the Eukaryotic Replicative Helicase at Lagging-Strand Protein Barriers Support the Steric Exclusion Model",
abstract = "Progression of DNA replication depends on the ability of the replisome complex to overcome nucleoprotein barriers. During eukaryotic replication, the CMG helicase translocates along the leading-strand template and unwinds the DNA double helix. While proteins bound to the leading-strand template efficiently block the helicase, the impact of lagging-strand protein obstacles on helicase translocation and replisome progression remains controversial. Here, we show that CMG and replisome progressions are impaired when proteins crosslinked to the lagging-strand template enhance the stability of duplex DNA. In contrast, proteins that exclusively interact with the lagging-strand template influence neither the translocation of isolated CMG nor replisome progression in Xenopus egg extracts. Our data imply that CMG completely excludes the lagging-strand template from the helicase central channel while unwinding DNA at the replication fork, which clarifies how two CMG helicases could freely cross one another during replication initiation and termination.",
author = "Kose, {Hazal B.} and Larsen, {Nicolai B.} and Duxin, {Julien P.} and Hasan Yardimci",
year = "2019",
doi = "10.1016/j.celrep.2019.01.086",
language = "English",
volume = "26",
pages = "2113--2125.e6",
journal = "Cell Reports",
issn = "2211-1247",
publisher = "Cell Press",
number = "8",

}

RIS

TY - JOUR

T1 - Dynamics of the Eukaryotic Replicative Helicase at Lagging-Strand Protein Barriers Support the Steric Exclusion Model

AU - Kose, Hazal B.

AU - Larsen, Nicolai B.

AU - Duxin, Julien P.

AU - Yardimci, Hasan

PY - 2019

Y1 - 2019

N2 - Progression of DNA replication depends on the ability of the replisome complex to overcome nucleoprotein barriers. During eukaryotic replication, the CMG helicase translocates along the leading-strand template and unwinds the DNA double helix. While proteins bound to the leading-strand template efficiently block the helicase, the impact of lagging-strand protein obstacles on helicase translocation and replisome progression remains controversial. Here, we show that CMG and replisome progressions are impaired when proteins crosslinked to the lagging-strand template enhance the stability of duplex DNA. In contrast, proteins that exclusively interact with the lagging-strand template influence neither the translocation of isolated CMG nor replisome progression in Xenopus egg extracts. Our data imply that CMG completely excludes the lagging-strand template from the helicase central channel while unwinding DNA at the replication fork, which clarifies how two CMG helicases could freely cross one another during replication initiation and termination.

AB - Progression of DNA replication depends on the ability of the replisome complex to overcome nucleoprotein barriers. During eukaryotic replication, the CMG helicase translocates along the leading-strand template and unwinds the DNA double helix. While proteins bound to the leading-strand template efficiently block the helicase, the impact of lagging-strand protein obstacles on helicase translocation and replisome progression remains controversial. Here, we show that CMG and replisome progressions are impaired when proteins crosslinked to the lagging-strand template enhance the stability of duplex DNA. In contrast, proteins that exclusively interact with the lagging-strand template influence neither the translocation of isolated CMG nor replisome progression in Xenopus egg extracts. Our data imply that CMG completely excludes the lagging-strand template from the helicase central channel while unwinding DNA at the replication fork, which clarifies how two CMG helicases could freely cross one another during replication initiation and termination.

U2 - 10.1016/j.celrep.2019.01.086

DO - 10.1016/j.celrep.2019.01.086

M3 - Journal article

C2 - 30784593

VL - 26

SP - 2113-2125.e6

JO - Cell Reports

JF - Cell Reports

SN - 2211-1247

IS - 8

ER -

ID: 214126560