Recognition of SUMO-modified PCNA requires tandem receptor motifs in Srs2.

Recognition of SUMO-modified PCNA requires tandem receptor motifs in Srs2.
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DOI:
10.1038/nature10883
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发表时间:
2012-02-29
期刊:
影响因子:
64.8
通讯作者:
Lima, Christopher D.
Lima, Christopher D.
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Armstrong, Anthony A.;Mohideen, Firaz;Lima, Christopher D.

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Ubiquitin (Ub) and ubiquitin-like (Ubl) modifiers such as SUMO mediate signal transduction through post-translational modification of substrate proteins in pathways that control differentiation, apoptosis, the cell cycle, and responses to stress such as the DNA damage response. In yeast, the proliferating cell nuclear antigen PCNA is modified by ubiquitin in response to DNA damage and by SUMO during S-phase. While Ub-PCNA can signal for recruitment of translesion DNA polymerases, SUMO-PCNA signals for recruitment of the anti-recombinogenic DNA helicase Srs2. It remains unclear how receptors such as Srs2 specifically recognize substrates after conjugation to Ub/Ubls. Here we show through structural, biochemical and functional studies that the Srs2 C-terminal domain harbors tandem receptor motifs that interact independently with PCNA and SUMO and that both motifs are required to specifically recognize SUMO-PCNA. The mechanism presented herein is pertinent to understanding how other receptors specifically recognize Ub/Ubl-modified substrates to facilitate signal transduction.
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