Crosstalk between SUMO and ubiquitin on PCNA is mediated by
recruitment of the helicase Srs2p.

J 2005

Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p.

PAPOULI, Efterpi, Shuhua CHEN, Adelina DAVIES, Diana HUTTNER, Lumir KREJCI et. al.

Základní údaje

Originální název

Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p.

Název česky

Komunikace mezi SUMO a ubiquitinem na PCNA je zprostředkována Srs2 proteinem

Autoři

PAPOULI, Efterpi (826 Velká Británie a Severní Irsko), Shuhua CHEN (826 Velká Británie a Severní Irsko), Adelina DAVIES (826 Velká Británie a Severní Irsko), Diana HUTTNER (826 Velká Británie a Severní Irsko), Lumir KREJCI (203 Česká republika, garant), Patrick SUNG (840 Spojené státy) a Helle ULRICH (276 Německo)

Vydání

Molecular Cell, 2005, 1097-2765

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 14.971

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000230282400011

Klíčová slova anglicky

PCNA; Srs2; SUMO; repair; replication

Štítky

PCNA, repair, replication, Srs2, SUMO

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 20. 6. 2009 06:39, doc. Mgr. Lumír Krejčí, Ph.D.

Anotace

ORIG CZ

V originále

Posttranslational modification of proliferating cell nuclear antigen (PCNA), an essential processivity clamp for DNA polymerases, by ubiquitin and SUMO contributes to the coordination of DNA replication, damage tolerance, and mutagenesis. Whereas ubiquitination in response to DNA damage promotes the bypass of replication-blocking lesions, sumoylation during S phase is damage independent. As both modifiers target the same site on PCNA, an antagonistic action of SUMO on ubiquitin-dependent DNA damage tolerance has been proposed. We now present evidence that the apparent negative effect of SUMO on lesion bypass is not due to competition with ubiquitination but is rather mediated by the helicase Srs2p, which affects genome stability by suppressing unscheduled homologous recombination. We show that Srs2p physically interacts with sumoylated PCNA, which contributes to the recruitment of the helicase to replication forks. Our findings suggest a mechanism by which SUMO and ubiquitin cooperatively control the choice of pathway for the processing of DNA lesions during replication.

Česky

Vliv post-translační modifikace PCNA na interakci s Srs2 proteinem

Citovat

PAPOULI, Efterpi, Shuhua CHEN, Adelina DAVIES, Diana HUTTNER, Lumir KREJCI, Patrick SUNG a Helle ULRICH. Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p. Molecular Cell. 2005, roč. 19, č. 1, s. 123-33, 10 s. ISSN 1097-2765.

@article{708615,
   author = {Papouli, Efterpi and Chen, Shuhua and Davies, Adelina and Huttner, Diana and Krejci, Lumir and Sung, Patrick and Ulrich, Helle},
   article_number = {1},
   keywords = {PCNA; Srs2; SUMO; repair; replication},
   language = {eng},
   issn = {1097-2765},
   journal = {Molecular Cell},
   title = {Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p.},
   url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&dopt=AbstractPlus&list_uids=15989970&query_hl=20&itool=pubmed_docsum},
   volume = {19},
   year = {2005}
}

TY  - JOUR
ID  - 708615
AU  - Papouli, Efterpi - Chen, Shuhua - Davies, Adelina - Huttner, Diana - Krejci, Lumir - Sung, Patrick - Ulrich, Helle
PY  - 2005
TI  - Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p.
JF  - Molecular Cell
VL  - 19
IS  - 1
SP  - 123-33
EP  - 123-33
SN  - 10972765
KW  - PCNA
KW  - Srs2
KW  - SUMO
KW  - repair
KW  - replication
UR  - http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&dopt=AbstractPlus&list_uids=15989970&query_hl=20&itool=pubmed_docsum
L2  - http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&dopt=AbstractPlus&list_uids=15989970&query_hl=20&itool=pubmed_docsum
N2  - Posttranslational modification of proliferating cell nuclear antigen (PCNA), an essential processivity clamp for DNA polymerases, by ubiquitin and SUMO contributes to the coordination of DNA replication, damage tolerance, and mutagenesis. Whereas ubiquitination in response to DNA damage promotes the bypass of replication-blocking lesions, sumoylation during S phase is damage independent. As both modifiers target the same site on PCNA, an antagonistic action of SUMO on ubiquitin-dependent DNA damage tolerance has been proposed. We now present evidence that the apparent negative effect of SUMO on lesion bypass is not due to competition with ubiquitination but is rather mediated by the helicase Srs2p, which affects genome stability by suppressing unscheduled homologous recombination. We show that Srs2p physically interacts with sumoylated PCNA, which contributes to the recruitment of the helicase to replication forks. Our findings suggest a mechanism by which SUMO and ubiquitin cooperatively control the choice of pathway for the processing of DNA lesions during replication.
ER  -

PAPOULI, Efterpi, Shuhua CHEN, Adelina DAVIES, Diana HUTTNER, Lumir KREJCI, Patrick SUNG a Helle ULRICH. Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p. \textit{Molecular Cell}. 2005, roč.~19, č.~1, s.~123-33, 10 s. ISSN~1097-2765.

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