Mitotic replisome disassembly depends on TRAIP ubiquitin ligase activity

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Mitotic replisome disassembly depends on TRAIP ubiquitin ligase activity. / Moreno, Sara Priego; Jones, Rebecca M; Poovathumkadavil, Divyasree; Scaramuzza, Shaun; Gambus, Agnieszka.

In: Life Science Alliance, Vol. 2, No. 2, e201900390, 12.04.2019.

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@article{6074aea3489d4aa0a91f122418baf3c1,
title = "Mitotic replisome disassembly depends on TRAIP ubiquitin ligase activity",
abstract = "We have shown previously that the process of replication machinery (replisome) disassembly at the termination of DNA replication forks in the S-phase is driven through polyubiquitylation of one of the replicative helicase subunits (Mcm7) by Cul2LRR1 ubiquitin ligase. Interestingly, upon inhibition of this pathway in Caenorhabditis elegans embryos, the replisomes retained on chromatin were unloaded in the subsequent mitosis. Here, we show that this mitotic replisome disassembly pathway exists in Xenopus laevis egg extract and we determine the first elements of its regulation. The mitotic disassembly pathway depends on the formation of K6- and K63-linked ubiquitin chains on Mcm7 by TRAIP ubiquitin ligase and the activity of p97/VCP protein segregase. Unlike in lower eukaryotes, however, it does not require SUMO modifications. Importantly, we also show that this process can remove all replisomes from mitotic chromatin, including stalled ones, which indicates a wide application for this pathway over being just a “backup” for terminated replisomes. Finally, we characterise the composition of the replisome retained on chromatin until mitosis.",
author = "Moreno, {Sara Priego} and Jones, {Rebecca M} and Divyasree Poovathumkadavil and Shaun Scaramuzza and Agnieszka Gambus",
year = "2019",
month = apr,
day = "12",
doi = "10.26508/lsa.201900390",
language = "English",
volume = "2",
journal = "Life Science Alliance",
issn = "2575-1077",
publisher = "Life Science Alliance LLC",
number = "2",

}

RIS

TY - JOUR

T1 - Mitotic replisome disassembly depends on TRAIP ubiquitin ligase activity

AU - Moreno, Sara Priego

AU - Jones, Rebecca M

AU - Poovathumkadavil, Divyasree

AU - Scaramuzza, Shaun

AU - Gambus, Agnieszka

PY - 2019/4/12

Y1 - 2019/4/12

N2 - We have shown previously that the process of replication machinery (replisome) disassembly at the termination of DNA replication forks in the S-phase is driven through polyubiquitylation of one of the replicative helicase subunits (Mcm7) by Cul2LRR1 ubiquitin ligase. Interestingly, upon inhibition of this pathway in Caenorhabditis elegans embryos, the replisomes retained on chromatin were unloaded in the subsequent mitosis. Here, we show that this mitotic replisome disassembly pathway exists in Xenopus laevis egg extract and we determine the first elements of its regulation. The mitotic disassembly pathway depends on the formation of K6- and K63-linked ubiquitin chains on Mcm7 by TRAIP ubiquitin ligase and the activity of p97/VCP protein segregase. Unlike in lower eukaryotes, however, it does not require SUMO modifications. Importantly, we also show that this process can remove all replisomes from mitotic chromatin, including stalled ones, which indicates a wide application for this pathway over being just a “backup” for terminated replisomes. Finally, we characterise the composition of the replisome retained on chromatin until mitosis.

AB - We have shown previously that the process of replication machinery (replisome) disassembly at the termination of DNA replication forks in the S-phase is driven through polyubiquitylation of one of the replicative helicase subunits (Mcm7) by Cul2LRR1 ubiquitin ligase. Interestingly, upon inhibition of this pathway in Caenorhabditis elegans embryos, the replisomes retained on chromatin were unloaded in the subsequent mitosis. Here, we show that this mitotic replisome disassembly pathway exists in Xenopus laevis egg extract and we determine the first elements of its regulation. The mitotic disassembly pathway depends on the formation of K6- and K63-linked ubiquitin chains on Mcm7 by TRAIP ubiquitin ligase and the activity of p97/VCP protein segregase. Unlike in lower eukaryotes, however, it does not require SUMO modifications. Importantly, we also show that this process can remove all replisomes from mitotic chromatin, including stalled ones, which indicates a wide application for this pathway over being just a “backup” for terminated replisomes. Finally, we characterise the composition of the replisome retained on chromatin until mitosis.

UR - http://www.scopus.com/inward/record.url?scp=85065704116&partnerID=8YFLogxK

U2 - 10.26508/lsa.201900390

DO - 10.26508/lsa.201900390

M3 - Article

VL - 2

JO - Life Science Alliance

JF - Life Science Alliance

SN - 2575-1077

IS - 2

M1 - e201900390

ER -