---
DOAJ_listed: '1'
OA_place: publisher
OA_type: gold
_id: '18253'
abstract:
- lang: eng
text: PCNA, the ring that encircles DNA maintaining the processivity of DNA polymerases,
is modified by ubiquitin and SUMO. Whereas ubiquitin is required for bypassing
lesions through the DNA damage tolerance (DDT) pathways, we show here that SUMOylation
represses another pathway, salvage recombination. The Srs2 helicase is recruited
to SUMOylated PCNA and prevents the salvage pathway from acting. The pathway can
be induced by overexpressing the PCNA unloader Elg1, or the homologous recombination
protein Rad52. Our results underscore the role of PCNA modifications in controlling
the various bypass and DNA repair mechanisms.
article_number: 00705-20
article_processing_charge: Yes
article_type: original
author:
- first_name: Matan
full_name: Arbel, Matan
last_name: Arbel
- first_name: Alexander
full_name: Bronstein, Alexander
id: 58f3726e-7cba-11ef-ad8b-e6e8cb3904e6
last_name: Bronstein
orcid: 0000-0001-9699-8730
- first_name: Soumitra
full_name: Sau, Soumitra
last_name: Sau
- first_name: Batia
full_name: Liefshitz, Batia
last_name: Liefshitz
- first_name: Martin
full_name: Kupiec, Martin
last_name: Kupiec
citation:
ama: Arbel M, Bronstein AM, Sau S, Liefshitz B, Kupiec M. Access to PCNA by Srs2
and Elg1 controls the choice between alternative repair pathways in Saccharomyces
cerevisiae. mBio. 2020;11(3). doi:10.1128/mbio.00705-20
apa: Arbel, M., Bronstein, A. M., Sau, S., Liefshitz, B., & Kupiec, M. (2020).
Access to PCNA by Srs2 and Elg1 controls the choice between alternative repair
pathways in Saccharomyces cerevisiae. MBio. American Society for Microbiology.
https://doi.org/10.1128/mbio.00705-20
chicago: Arbel, Matan, Alex M. Bronstein, Soumitra Sau, Batia Liefshitz, and Martin
Kupiec. “Access to PCNA by Srs2 and Elg1 Controls the Choice between Alternative
Repair Pathways in Saccharomyces Cerevisiae.” MBio. American Society for
Microbiology, 2020. https://doi.org/10.1128/mbio.00705-20.
ieee: M. Arbel, A. M. Bronstein, S. Sau, B. Liefshitz, and M. Kupiec, “Access to
PCNA by Srs2 and Elg1 controls the choice between alternative repair pathways
in Saccharomyces cerevisiae,” mBio, vol. 11, no. 3. American Society for
Microbiology, 2020.
ista: Arbel M, Bronstein AM, Sau S, Liefshitz B, Kupiec M. 2020. Access to PCNA
by Srs2 and Elg1 controls the choice between alternative repair pathways in Saccharomyces
cerevisiae. mBio. 11(3), 00705-20.
mla: Arbel, Matan, et al. “Access to PCNA by Srs2 and Elg1 Controls the Choice between
Alternative Repair Pathways in Saccharomyces Cerevisiae.” MBio, vol. 11,
no. 3, 00705-20, American Society for Microbiology, 2020, doi:10.1128/mbio.00705-20.
short: M. Arbel, A.M. Bronstein, S. Sau, B. Liefshitz, M. Kupiec, MBio 11 (2020).
date_created: 2024-10-08T13:06:43Z
date_published: 2020-06-01T00:00:00Z
date_updated: 2024-10-15T10:50:42Z
day: '01'
doi: 10.1128/mbio.00705-20
extern: '1'
external_id:
pmid:
- '32371600'
intvolume: ' 11'
issue: '3'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1128/mbio.00705-20
month: '06'
oa: 1
oa_version: Published Version
pmid: 1
publication: mBio
publication_identifier:
eissn:
- 2150-7511
issn:
- 2161-2129
publication_status: published
publisher: American Society for Microbiology
quality_controlled: '1'
scopus_import: '1'
status: public
title: Access to PCNA by Srs2 and Elg1 controls the choice between alternative repair
pathways in Saccharomyces cerevisiae
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 11
year: '2020'
...
---
DOAJ_listed: '1'
_id: '18275'
abstract:
- lang: eng
text: "Homologous recombination (HR) is a mechanism that repairs a variety of DNA
lesions. Under certain circumstances, however, HR can generate intermediates that
can interfere with other cellular processes such as DNA transcription or replication.
Cells have therefore developed pathways that abolish undesirable HR intermediates.
The Saccharomyces cerevisiae yeast Srs2 helicase has a major role in one of these
pathways. Srs2 also works during DNA replication and interacts with the clamp
PCNA. The relative importance of Srs2’s helicase activity, Rad51 removal function,
and PCNA interaction in genome stability remains unclear. We created a new SRS2
allele [srs2(1-850)] that lacks the whole C terminus, containing the interaction
site for Rad51 and PCNA and interactions with many other proteins. Thus, the new
allele encodes an Srs2 protein bearing only the activity of the DNA helicase.
We find that the interactions of Srs2 with Rad51 and PCNA are dispensable for
the main role of Srs2 in the repair of DNA damage in vegetative cells and for
proper completion of meiosis. On the other hand, it has been shown that in cells
impaired for the DNA damage tolerance (DDT) pathways, Srs2 generates toxic intermediates
that lead to DNA damage sensitivity; we show that this negative Srs2 activity
requires the C terminus of Srs2. Dissection of the genetic interactions of the
srs2(1-850) allele suggest a role for Srs2’s helicase activity in sister chromatid
cohesion. Our results also indicate that Srs2’s function becomes more central
in diploid cells.\r\nIMPORTANCE Homologous recombination (HR) is a key mechanism
that repairs damaged DNA. However, this process has to be tightly regulated; failure
to regulate it can lead to genome instability. The Srs2 helicase is considered
a regulator of HR; it was shown to be able to evict the recombinase Rad51 from
DNA. Cells lacking Srs2 exhibit sensitivity to DNA-damaging agents, and in some
cases, they display defects in DNA replication. The relative roles of the helicase
and Rad51 removal activities of Srs2 in genome stability remain unclear. To address
this question, we created a new Srs2 mutant which has only the DNA helicase domain.
Our study shows that only the DNA helicase domain is needed to deal with DNA damage
and assist in DNA replication during vegetative growth and in meiosis. Thus, our
findings shift the view on the role of Srs2 in the maintenance of genome integrity."
article_number: e01192-18
article_processing_charge: No
author:
- first_name: Alexander
full_name: Bronstein, Alexander
id: 58f3726e-7cba-11ef-ad8b-e6e8cb3904e6
last_name: Bronstein
orcid: 0000-0001-9699-8730
- first_name: Lihi
full_name: Gershon, Lihi
last_name: Gershon
- first_name: Gilad
full_name: Grinberg, Gilad
last_name: Grinberg
- first_name: Elisa
full_name: Alonso-Perez, Elisa
last_name: Alonso-Perez
- first_name: Martin
full_name: Kupiec, Martin
last_name: Kupiec
citation:
ama: Bronstein AM, Gershon L, Grinberg G, Alonso-Perez E, Kupiec M. The main role
of Srs2 in DNA repair depends on its helicase activity, rather than on its interactions
with PCNA or Rad51. mBio. 2018;9(4). doi:10.1128/mbio.01192-18
apa: Bronstein, A. M., Gershon, L., Grinberg, G., Alonso-Perez, E., & Kupiec,
M. (2018). The main role of Srs2 in DNA repair depends on its helicase activity,
rather than on its interactions with PCNA or Rad51. MBio. American Society
for Microbiology. https://doi.org/10.1128/mbio.01192-18
chicago: Bronstein, Alex M., Lihi Gershon, Gilad Grinberg, Elisa Alonso-Perez, and
Martin Kupiec. “The Main Role of Srs2 in DNA Repair Depends on Its Helicase Activity,
Rather than on Its Interactions with PCNA or Rad51.” MBio. American Society
for Microbiology, 2018. https://doi.org/10.1128/mbio.01192-18.
ieee: A. M. Bronstein, L. Gershon, G. Grinberg, E. Alonso-Perez, and M. Kupiec,
“The main role of Srs2 in DNA repair depends on its helicase activity, rather
than on its interactions with PCNA or Rad51,” mBio, vol. 9, no. 4. American
Society for Microbiology, 2018.
ista: Bronstein AM, Gershon L, Grinberg G, Alonso-Perez E, Kupiec M. 2018. The main
role of Srs2 in DNA repair depends on its helicase activity, rather than on its
interactions with PCNA or Rad51. mBio. 9(4), e01192-18.
mla: Bronstein, Alex M., et al. “The Main Role of Srs2 in DNA Repair Depends on
Its Helicase Activity, Rather than on Its Interactions with PCNA or Rad51.” MBio,
vol. 9, no. 4, e01192-18, American Society for Microbiology, 2018, doi:10.1128/mbio.01192-18.
short: A.M. Bronstein, L. Gershon, G. Grinberg, E. Alonso-Perez, M. Kupiec, MBio
9 (2018).
date_created: 2024-10-09T07:44:09Z
date_published: 2018-07-17T00:00:00Z
date_updated: 2024-12-19T12:43:33Z
day: '17'
doi: 10.1128/mbio.01192-18
extern: '1'
intvolume: ' 9'
issue: '4'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1128/mbio.01192-18
month: '07'
oa: 1
oa_version: Published Version
publication: mBio
publication_identifier:
eissn:
- 2150-7511
publication_status: published
publisher: American Society for Microbiology
quality_controlled: '1'
scopus_import: '1'
status: public
title: The main role of Srs2 in DNA repair depends on its helicase activity, rather
than on its interactions with PCNA or Rad51
type: journal_article
user_id: 3E5EF7F0-F248-11E8-B48F-1D18A9856A87
volume: 9
year: '2018'
...