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TitleMolecular architecture of the Ub-PCNA/Pol η complex bound to DNA.
Journal, issue, pagesSci Rep, Vol. 5, Page 15759, Year 2015
Publish dateOct 27, 2015
AuthorsWilson C Y Lau / Yinyin Li / Qinfen Zhang / Michael S Y Huen /
PubMed AbstractTranslesion synthesis (TLS) is the mechanism by which DNA polymerases replicate through unrepaired DNA lesions. TLS is activated by monoubiquitination of the homotrimeric proliferating cell nuclear ...Translesion synthesis (TLS) is the mechanism by which DNA polymerases replicate through unrepaired DNA lesions. TLS is activated by monoubiquitination of the homotrimeric proliferating cell nuclear antigen (PCNA) at lysine-164, followed by the switch from replicative to specialized polymerases at DNA damage sites. Pol η belongs to the Y-Family of specialized polymerases that can efficiently bypass UV-induced lesions. Like other members of the Y-Family polymerases, its recruitment to the damaged sites is mediated by the interaction with monoubiquitinated PCNA (Ub-PCNA) via its ubiquitin-binding domain and non-canonical PCNA-interacting motif in the C-terminal region. The structural determinants underlying the direct recognition of Ub-PCNA by Pol η, or Y-Family polymerases in general, remain largely unknown. Here we report a structure of the Ub-PCNA/Pol η complex bound to DNA determined by single-particle electron microscopy (EM). The overall obtained structure resembles that of the editing PCNA/PolB complex. Analysis of the map revealed the conformation of ubiquitin that binds the C-terminal domain of Pol η. Our present study suggests that the Ub-PCNA/Pol η interaction requires the formation of a structured binding interface, which is dictated by the inherent flexibility of Ub-PCNA.
External linksSci Rep / PubMed:26503230 / PubMed Central
MethodsEM (single particle)
Resolution22.0 Å
Structure data

6339

3ja9

3jaa

EMDB-6339: Molecular architecture of the Ub-PCNA/Pol eta complex bound to DNA
PDB-3ja9: Structure of native human PCNA
PDB-3jaa: HUMAN DNA POLYMERASE ETA in COMPLEX WITH NORMAL DNA AND INCO NUCLEOTIDE (NRM)
Method: EM (single particle) / Resolution: 22.0 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-DZ4:
2'-deoxy-5'-O-[(R)-hydroxy{[(R)-hydroxy(phosphonooxy)phosphoryl]amino}phosphoryl]adenosine

ChemComp-MG:
Unknown entry

ChemComp-GOL:
GLYCEROL

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsDNA BINDING PROTEIN / DNA / REPLICATION / PROCESSIVITY / ONCOGENE / DNA-BINDING SYSTEMIC LUPUS ERYTHEMATOSUS / TRANSFERASE/DNA / POL ETA / POLYMERASE / THYMINE DIMER / CPD / XPV / XERODERMA PIGM VARIANT / DNA DAMAGE / TRANSFERASE-DNA COMPLEX

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