Structure of monoubiquitinated PCNA and implications for translesion synthesis and DNA polymerase exchange
The monoubiquitination of processivity factor PCNA at Lys164 in yeast leads to exchange of a replicative DNA polymerase with a translesion one. Now a functional, split version of monoubiquitinated PCNA is developed and its crystal structure shows that the ubiquitin moiety is located at the back face...
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| Published in: | Nature Structural & Molecular Biology Vol. 17; no. 4; pp. 479 - 484 |
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| Abstract | The monoubiquitination of processivity factor PCNA at Lys164 in yeast leads to exchange of a replicative DNA polymerase with a translesion one. Now a functional, split version of monoubiquitinated PCNA is developed and its crystal structure shows that the ubiquitin moiety is located at the back face of the PCNA ring and does not cause large conformational changes in PCNA.
DNA synthesis by classical polymerases can be blocked by many lesions. These blocks are overcome by translesion synthesis, whereby the stalled classical, replicative polymerase is replaced by a nonclassical polymerase. In eukaryotes this polymerase exchange requires proliferating cell nuclear antigen (PCNA) monoubiquitination. To better understand the polymerase exchange, we developed a means of producing monoubiquitinated PCNA, by splitting the protein into two self-assembling polypeptides. We determined the X-ray crystal structure of monoubiquitinated PCNA and found that the ubiquitin moieties are located on the back face of PCNA and interact with it through their canonical hydrophobic surface. Moreover, the attachment of ubiquitin does not change PCNA's conformation. We propose that PCNA ubiquitination facilitates nonclassical polymerase recruitment to the back of PCNA by forming a new binding surface for nonclassical polymerases, consistent with a 'tool belt' model of the polymerase exchange. |
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| AbstractList | DNA synthesis by classical polymerases can be blocked by many lesions. These blocks are overcome by translesion synthesis, whereby the stalled classical, replicative polymerase is replaced by a non-classical polymerase. In eukaryotes, this polymerase exchange requires PCNA monoubiquitination. To better understand the polymerase exchange, we have developed a novel means of producing monoubiquitinated PCNA, by splitting the protein into two self-assembling polypeptides. We determined the X-ray crystal structure of monoubiquitinated PCNA and found that the ubiquitin moieties are located on the back face of PCNA and interact with it via their canonical hydrophobic surface. Moreover, the attachment of ubiquitin does not change PCNA’s conformation. We propose that PCNA ubiquitination facilitates non-classical polymerase recruitment to the back of PCNA by forming a new binding surface for non-classical polymerases, consistent with a “tool belt” model of the polymerase exchange. DNA synthesis by classical polymerases can be blocked by many lesions. These blocks are overcome by translesion synthesis, whereby the stalled classical, replicative polymerase is replaced by a nonclassical polymerase. In eukaryotes this polymerase exchange requires proliferating cell nuclear antigen (PCNA) monoubiquitination. To better understand the polymerase exchange, we developed a means of producing monoubiquitinated PCNA, by splitting the protein into two self-assembling polypeptides. We determined the X-ray crystal structure of monoubiquitinated PCNA and found that the ubiquitin moieties are located on the back face of PCNA and interact with it through their canonical hydrophobic surface. Moreover, the attachment of ubiquitin does not change PCNA's conformation. We propose that PCNA ubiquitination facilitates nonclassical polymerase recruitment to the back of PCNA by forming a new binding surface for nonclassical polymerases, consistent with a 'tool belt' model of the polymerase exchange. The monoubiquitination of processivity factor PCNA at Lys164 in yeast leads to exchange of a replicative DNA polymerase with a translesion one. Now a functional, split version of monoubiquitinated PCNA is developed and its crystal structure shows that the ubiquitin moiety is located at the back face of the PCNA ring and does not cause large conformational changes in PCNA. DNA synthesis by classical polymerases can be blocked by many lesions. These blocks are overcome by translesion synthesis, whereby the stalled classical, replicative polymerase is replaced by a nonclassical polymerase. In eukaryotes this polymerase exchange requires proliferating cell nuclear antigen (PCNA) monoubiquitination. To better understand the polymerase exchange, we developed a means of producing monoubiquitinated PCNA, by splitting the protein into two self-assembling polypeptides. We determined the X-ray crystal structure of monoubiquitinated PCNA and found that the ubiquitin moieties are located on the back face of PCNA and interact with it through their canonical hydrophobic surface. Moreover, the attachment of ubiquitin does not change PCNA's conformation. We propose that PCNA ubiquitination facilitates nonclassical polymerase recruitment to the back of PCNA by forming a new binding surface for nonclassical polymerases, consistent with a 'tool belt' model of the polymerase exchange. DNA synthesis by classical polymerases can be blocked by many lesions. These blocks are overcome by translesion synthesis, whereby the stalled classical, replicative polymerase is replaced by a nonclassical polymerase. In eukaryotes this polymerase exchange requires proliferating cell nuclear antigen (PCNA) monoubiquitination. To better understand the polymerase exchange, we developed a means of producing monoubiquitinated PCNA, by splitting the protein into two self-assembling polypeptides. We determined the X-ray crystal structure of monoubiquitinated PCNA and found that the ubiquitin moieties are located on the back face of PCNA and interact with it through their canonical hydrophobic surface. Moreover, the attachment of ubiquitin does not change PCNA's conformation. We propose that PCNA ubiquitination facilitates nonclassical polymerase recruitment to the back of PCNA by forming a new binding surface for nonclassical polymerases, consistent with a 'tool belt' model of the polymerase exchange.[PUBLICATION ABSTRACT] |
| Audience | Academic |
| Author | Ramaswamy, S Freudenthal, Bret D Washington, M Todd Gakhar, Lokesh |
| AuthorAffiliation | 1 Department of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242 2 Protein Crystallography Facility, University of Iowa College of Medicine, Iowa City, IA 52242 |
| AuthorAffiliation_xml | – name: 2 Protein Crystallography Facility, University of Iowa College of Medicine, Iowa City, IA 52242 – name: 1 Department of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242 |
| Author_xml | – givenname: Bret D surname: Freudenthal fullname: Freudenthal, Bret D organization: Department of Biochemistry, University of Iowa College of Medicine – givenname: S surname: Ramaswamy fullname: Ramaswamy, S organization: Department of Biochemistry, University of Iowa College of Medicine – givenname: M Todd surname: Washington fullname: Washington, M Todd organization: Department of Biochemistry, University of Iowa College of Medicine – givenname: Lokesh surname: Gakhar fullname: Gakhar, Lokesh organization: Protein Crystallography Facility, University of Iowa College of Medicine |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/20305653$$D View this record in MEDLINE/PubMed |
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| Snippet | The monoubiquitination of processivity factor PCNA at Lys164 in yeast leads to exchange of a replicative DNA polymerase with a translesion one. Now a... DNA synthesis by classical polymerases can be blocked by many lesions. These blocks are overcome by translesion synthesis, whereby the stalled classical,... |
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| SubjectTerms | 631/337/1427/2354 631/45/535 Antigens Biochemistry Biological Microscopy Biomedical and Life Sciences Causes of Chemical synthesis Crystallography, X-Ray Deoxyribonucleic acid DNA DNA damage DNA polymerases DNA Repair DNA-Directed DNA Polymerase - metabolism Genetic aspects Ion exchange Lesions Life Sciences Membrane Biology Models, Molecular Physiological aspects Polymers Proliferating Cell Nuclear Antigen - chemistry Proliferating Cell Nuclear Antigen - metabolism Protein Conformation Protein Structure Ubiquitin Ubiquitination |
| Title | Structure of monoubiquitinated PCNA and implications for translesion synthesis and DNA polymerase exchange |
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