S177G Mutant of Yeast PCNAS177G Mutant of Yeast PCNA

Structural highlights

6cx2 is a 1 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.101Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PCNA_YEAST This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Involved in DNA repair.[1] [2]

Publication Abstract from PubMed

Proliferating cell nuclear antigen (PCNA) plays an essential role in DNA replication and repair by interacting with a large number of proteins involved in these processes. Two amino acid substitutions in PCNA, both located at the subunit interface, have previously been shown to block translesion synthesis (TLS), a pathway for bypassing DNA damage during replication. To better understand the role of the subunit interface in TLS, we used random mutagenesis to generate a set of 33 PCNA mutants with substitutions at the subunit interface. We assayed the full set of mutants for viability and sensitivity to ultraviolet (UV) radiation. We then selected a subset of 17 mutants and measured their rates of cell growth, spontaneous mutagenesis, and UV-induced mutagenesis. All except three of these 17 mutants were partially or completely defective in induced mutagenesis, which indicates a partial or complete loss of TLS. These results demonstrate that the integrity of the subunit interface of PCNA is essential for efficient TLS and that even conservative substitutions have the potential to disrupt this process.

Identification of New Mutations at the PCNA Subunit Interface that Block Translesion Synthesis.,Kondratick CM, Boehm EM, Dieckman LM, Powers KT, Sanchez JC, Mueting SR, Washington MT PLoS One. 2016 Jun 3;11(6):e0157023. doi: 10.1371/journal.pone.0157023., eCollection 2016. PMID:27258147[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Haracska L, Kondratick CM, Unk I, Prakash S, Prakash L. Interaction with PCNA is essential for yeast DNA polymerase eta function. Mol Cell. 2001 Aug;8(2):407-15. PMID:11545742
  2. Hoege C, Pfander B, Moldovan GL, Pyrowolakis G, Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature. 2002 Sep 12;419(6903):135-41. PMID:12226657 doi:10.1038/nature00991
  3. Kondratick CM, Boehm EM, Dieckman LM, Powers KT, Sanchez JC, Mueting SR, Washington MT. Identification of New Mutations at the PCNA Subunit Interface that Block Translesion Synthesis. PLoS One. 2016 Jun 3;11(6):e0157023. doi: 10.1371/journal.pone.0157023., eCollection 2016. PMID:27258147 doi:http://dx.doi.org/10.1371/journal.pone.0157023

6cx2, resolution 3.10Å

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