3V61

Structure of S. cerevisiae PCNA conjugated to SUMO on lysine 164

Summary for 3V61

• Entry DOI: 10.2210/pdb3v61/pdb
• Related: 3V60 3V62
• Descriptor: Ubiquitin-like protein SMT3, Proliferating cell nuclear antigen, BARIUM ION, ... (5 entities in total)
• Functional Keywords: ubiquitin-like protein pcna, post-translational modification, dna replication, dna damage response, srs2, nem modification on pcna cys22 and cys81, nuclear, protein binding-dna binding protein complex, protein binding/dna binding protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Nucleus: P15873
• Total number of polymer chains: 2
• Total formula weight: 40627.40

Authors

Armstrong, A.A.,Mohideen, F.,Lima, C.D. (deposition date: 2011-12-18, release date: 2012-02-29, Last modification date: 2023-09-13)

Primary citation

Armstrong, A.A.,Mohideen, F.,Lima, C.D.
Recognition of SUMO-modified PCNA requires tandem receptor motifs in Srs2.
Nature, 483:59-63, 2012

PubMed Abstract: Ubiquitin (Ub) and ubiquitin-like (Ubl) modifiers such as SUMO (also known as Smt3 in Saccharomyces cerevisiae) mediate signal transduction through post-translational modification of substrate proteins in pathways that control differentiation, apoptosis and the cell cycle, and responses to stress such as the DNA damage response. In yeast, the proliferating cell nuclear antigen PCNA (also known as Pol30) is modified by ubiquitin in response to DNA damage and by SUMO during S phase. Whereas 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 and Ubls. Here we show, through structural, biochemical and functional studies, that the Srs2 carboxy-terminal domain harbours tandem receptor motifs that interact independently with PCNA and SUMO and that both motifs are required to recognize SUMO-PCNA specifically. The mechanism presented is pertinent to understanding how other receptors specifically recognize Ub- and Ubl-modified substrates to facilitate signal transduction.

PubMed: 22382979
DOI: 10.1038/nature10883

Experimental method

X-RAY DIFFRACTION (2.8 Å)