Rad9/53BP1 protects stalled replication forks from degradation in Mec1/ATR-defective cells

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

Standard

Rad9/53BP1 protects stalled replication forks from degradation in Mec1/ATR-defective cells. / Villa, Matteo; Bonetti, Diego; Carraro, Massimo; Longhese, Maria Pia.

In: EMBO Reports, Vol. 19, No. 2, 2018, p. 351-367.

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

Harvard

Villa, M, Bonetti, D, Carraro, M & Longhese, MP 2018, 'Rad9/53BP1 protects stalled replication forks from degradation in Mec1/ATR-defective cells', EMBO Reports, vol. 19, no. 2, pp. 351-367. https://doi.org/10.15252/embr.201744910

APA

Villa, M., Bonetti, D., Carraro, M., & Longhese, M. P. (2018). Rad9/53BP1 protects stalled replication forks from degradation in Mec1/ATR-defective cells. EMBO Reports, 19(2), 351-367. https://doi.org/10.15252/embr.201744910

Vancouver

Villa M, Bonetti D, Carraro M, Longhese MP. Rad9/53BP1 protects stalled replication forks from degradation in Mec1/ATR-defective cells. EMBO Reports. 2018;19(2):351-367. https://doi.org/10.15252/embr.201744910

Author

Villa, Matteo ; Bonetti, Diego ; Carraro, Massimo ; Longhese, Maria Pia. / Rad9/53BP1 protects stalled replication forks from degradation in Mec1/ATR-defective cells. In: EMBO Reports. 2018 ; Vol. 19, No. 2. pp. 351-367.

Bibtex

@article{56b76bd59bd744938aed2d499f431234,
title = "Rad9/53BP1 protects stalled replication forks from degradation in Mec1/ATR-defective cells",
abstract = "Nucleolytic processing by nucleases can be a relevant mechanism to allow repair/restart of stalled replication forks. However, nuclease action needs to be controlled to prevent overprocessing of damaged replication forks that can be detrimental to genome stability. The checkpoint protein Rad9/53BP1 is known to limit nucleolytic degradation (resection) of DNA double-strand breaks (DSBs) in both yeast and mammals. Here, we show that loss of the inhibition that Rad9 exerts on resection exacerbates the sensitivity to replication stress of Mec1/ATR-defective yeast cells by exposing stalled replication forks to Dna2-dependent degradation. This Rad9 protective function is independent of checkpoint activation and relies mainly on Rad9-Dpb11 interaction. We propose that Rad9/53BP1 supports cell viability by protecting stalled replication forks from extensive resection when the intra-S checkpoint is not fully functional.",
keywords = "Cell Cycle Proteins/metabolism, DNA Replication, Intracellular Signaling Peptides and Proteins/deficiency, Microbial Viability, Protein-Serine-Threonine Kinases/deficiency, Saccharomyces cerevisiae/genetics, Saccharomyces cerevisiae Proteins/metabolism, Stress, Physiological, Tumor Suppressor p53-Binding Protein 1/metabolism",
author = "Matteo Villa and Diego Bonetti and Massimo Carraro and Longhese, {Maria Pia}",
note = "{\textcopyright} 2018 The Authors.",
year = "2018",
doi = "10.15252/embr.201744910",
language = "English",
volume = "19",
pages = "351--367",
journal = "E M B O Reports",
issn = "1469-221X",
publisher = "Wiley-Blackwell",
number = "2",

}

RIS

TY - JOUR

T1 - Rad9/53BP1 protects stalled replication forks from degradation in Mec1/ATR-defective cells

AU - Villa, Matteo

AU - Bonetti, Diego

AU - Carraro, Massimo

AU - Longhese, Maria Pia

N1 - © 2018 The Authors.

PY - 2018

Y1 - 2018

N2 - Nucleolytic processing by nucleases can be a relevant mechanism to allow repair/restart of stalled replication forks. However, nuclease action needs to be controlled to prevent overprocessing of damaged replication forks that can be detrimental to genome stability. The checkpoint protein Rad9/53BP1 is known to limit nucleolytic degradation (resection) of DNA double-strand breaks (DSBs) in both yeast and mammals. Here, we show that loss of the inhibition that Rad9 exerts on resection exacerbates the sensitivity to replication stress of Mec1/ATR-defective yeast cells by exposing stalled replication forks to Dna2-dependent degradation. This Rad9 protective function is independent of checkpoint activation and relies mainly on Rad9-Dpb11 interaction. We propose that Rad9/53BP1 supports cell viability by protecting stalled replication forks from extensive resection when the intra-S checkpoint is not fully functional.

AB - Nucleolytic processing by nucleases can be a relevant mechanism to allow repair/restart of stalled replication forks. However, nuclease action needs to be controlled to prevent overprocessing of damaged replication forks that can be detrimental to genome stability. The checkpoint protein Rad9/53BP1 is known to limit nucleolytic degradation (resection) of DNA double-strand breaks (DSBs) in both yeast and mammals. Here, we show that loss of the inhibition that Rad9 exerts on resection exacerbates the sensitivity to replication stress of Mec1/ATR-defective yeast cells by exposing stalled replication forks to Dna2-dependent degradation. This Rad9 protective function is independent of checkpoint activation and relies mainly on Rad9-Dpb11 interaction. We propose that Rad9/53BP1 supports cell viability by protecting stalled replication forks from extensive resection when the intra-S checkpoint is not fully functional.

KW - Cell Cycle Proteins/metabolism

KW - DNA Replication

KW - Intracellular Signaling Peptides and Proteins/deficiency

KW - Microbial Viability

KW - Protein-Serine-Threonine Kinases/deficiency

KW - Saccharomyces cerevisiae/genetics

KW - Saccharomyces cerevisiae Proteins/metabolism

KW - Stress, Physiological

KW - Tumor Suppressor p53-Binding Protein 1/metabolism

U2 - 10.15252/embr.201744910

DO - 10.15252/embr.201744910

M3 - Journal article

C2 - 29301856

VL - 19

SP - 351

EP - 367

JO - E M B O Reports

JF - E M B O Reports

SN - 1469-221X

IS - 2

ER -

ID: 241940552