RAD18-independent ubiquitination of proliferating-cell nuclear antigen in the avian cell line DT40
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
Standard
RAD18-independent ubiquitination of proliferating-cell nuclear antigen in the avian cell line DT40. / Simpson, Laura J.; Ross, Anna Laura; Szüts, Dávid; Alviani, Cherry A.; Oestergaard, Vibe H.; Patel, Ketan J.; Sale, Julian E.
I: EMBO Reports, Bind 7, Nr. 9, 01.09.2006, s. 927-932.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - RAD18-independent ubiquitination of proliferating-cell nuclear antigen in the avian cell line DT40
AU - Simpson, Laura J.
AU - Ross, Anna Laura
AU - Szüts, Dávid
AU - Alviani, Cherry A.
AU - Oestergaard, Vibe H.
AU - Patel, Ketan J.
AU - Sale, Julian E.
PY - 2006/9/1
Y1 - 2006/9/1
N2 - Ubiquitination of proliferating-cell nuclear antigen (PCNA) at K164 by RAD6/RAD18 has a key role in DNA damage tolerance in yeast. Here, we report on the first genetic study of this modification in a vertebrate cell. As in yeast, mutation of K164 of PCNA to arginine in the avian cell line DT40 results in sensitivity to DNA damage but, by contrast, the DT40 pcnaK164R mutant is more sensitive than the rad18 mutant. Consistent with this, we show the presence of residual ubiquitination of PCNA at K164 in the absence of functional RAD18, suggesting the presence of an alternate PCNA ubiquitinating enzyme in DT40. Furthermore, RAD18 and PCNA K164 have non-overlapping roles in the suppression of sister chromatid exchange in DT40, showing that RAD18 has other functions that do not involve the ubiquitination of PCNA.
AB - Ubiquitination of proliferating-cell nuclear antigen (PCNA) at K164 by RAD6/RAD18 has a key role in DNA damage tolerance in yeast. Here, we report on the first genetic study of this modification in a vertebrate cell. As in yeast, mutation of K164 of PCNA to arginine in the avian cell line DT40 results in sensitivity to DNA damage but, by contrast, the DT40 pcnaK164R mutant is more sensitive than the rad18 mutant. Consistent with this, we show the presence of residual ubiquitination of PCNA at K164 in the absence of functional RAD18, suggesting the presence of an alternate PCNA ubiquitinating enzyme in DT40. Furthermore, RAD18 and PCNA K164 have non-overlapping roles in the suppression of sister chromatid exchange in DT40, showing that RAD18 has other functions that do not involve the ubiquitination of PCNA.
UR - http://www.scopus.com/inward/record.url?scp=33749510488&partnerID=8YFLogxK
U2 - 10.1038/sj.embor.7400777
DO - 10.1038/sj.embor.7400777
M3 - Journal article
C2 - 16888649
AN - SCOPUS:33749510488
VL - 7
SP - 927
EP - 932
JO - E M B O Reports
JF - E M B O Reports
SN - 1469-221X
IS - 9
ER -
ID: 238744187