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This paper shows that the relative activities and amounts of replicative versus lesion-bypass DNA polymerases (Pol III and DinB) in the cell influence the mutation rate during replication.
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Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP
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0034666193
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Two novel human and mouse DNA polymerases of the pol X family
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Evidence that replication fork components catalyze establishment of cohesion between sister chromatids
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Carson D.R., Christman M.F. Evidence that replication fork components catalyze establishment of cohesion between sister chromatids. Proc. Natl. Acad. Sci. USA. 98:2001;8270-8275.
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0034714096
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DNA polymerase lambda (Pol λ), a novel eukaryotic DNA polymerase with a potential role in meiosis
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Garcia-Diaz M., Dominguez O., Lopez-Fernandez L.A., de Lera L.T., Saniger M.L., Ruiz J.F., Parraga M., Garcia-Ortiz M.J., Kirchhoff T., del Mazo J.et al. DNA polymerase lambda (Pol λ), a novel eukaryotic DNA polymerase with a potential role in meiosis. J. Mol. Biol. 301:2000;851-867.
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0035997344
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This is the most up-to-date review article of the X and Y family polymerases.
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Goodman M.F. Error-prone repair DNA polymerases in prokaryotes and eukaryotes. Annu. Rev. Biochem. 71:2002;17-50 This is the most up-to-date review article of the X and Y family polymerases.
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Goodman, M.F.1
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Expression of error-prone polymerases in BL2 cells activated for Ig somatic hypermutation
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This paper provides evidence for the role of Y-family polymerases in somatic hypermutation.
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Poltoratsky V., Woo C.J., Tippin B., Martin A., Goodman M.F., Scharff M.D. Expression of error-prone polymerases in BL2 cells activated for Ig somatic hypermutation. Proc. Natl. Acad. Sci. USA. 98:2001;7976-7981 This paper provides evidence for the role of Y-family polymerases in somatic hypermutation.
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Poltoratsky, V.1
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Martin, A.4
Goodman, M.F.5
Scharff, M.D.6
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36
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Induction of somatic hypermutation in immunoglobulin genes is dependent on DNA polymerase iota
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Faili A., Aoufouchi S., Flatter E., Gueranger Q., Reynaud C.A., Weill J.C. Induction of somatic hypermutation in immunoglobulin genes is dependent on DNA polymerase iota. Nature. 419:2002;944-947.
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Faili, A.1
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Weill, J.C.6
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37
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0034857266
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Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classic polymerase catalytic domain
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The crystal structure of the Dbh1 catalytic core is the first to be elucidated of the Y-family polymerases. This structure suggests that the Y-family polymerase is in a 'closed' active conformation even in the absence of substrate.
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Zhou B.L., Pata J.D., Steitz T.A. Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classic polymerase catalytic domain. Mol. Cell. 8:2001;427-437 The crystal structure of the Dbh1 catalytic core is the first to be elucidated of the Y-family polymerases. This structure suggests that the Y-family polymerase is in a 'closed' active conformation even in the absence of substrate.
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Mol. Cell
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Zhou, B.L.1
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Steitz, T.A.3
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38
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0034847259
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Structure of the catalytic core of S. cerevisiae DNA polymerase η: Implications for translesion DNA synthesis
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This paper reports the crystal structure of a large fragment of yeast Pol η, the homolog of human XP-V protein implicated in skin cancer. It is also the first structure of a eukaryotic Y-family polymerase.
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Trincao J., Johnson R.E., Escalante C.R., Prakash S., Prakash L., Aggarwal A.K. Structure of the catalytic core of S. cerevisiae DNA polymerase η: implications for translesion DNA synthesis. Mol. Cell. 8:2001;417-426 This paper reports the crystal structure of a large fragment of yeast Pol η, the homolog of human XP-V protein implicated in skin cancer. It is also the first structure of a eukaryotic Y-family polymerase.
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Mol. Cell
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Trincao, J.1
Johnson, R.E.2
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Prakash, S.4
Prakash, L.5
Aggarwal, A.K.6
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40
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0035812849
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Crystal structure of a Y-family DNA polymerase in action: A mechanism for error-prone and lesion-bypass replication
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The crystal structures of Dpo4-DNA complexes revealed the details of protein-DNA interactions and a mechanism by which the Y-family polymerases perform low-fidelity and translesion DNA synthesis.
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Ling H., Boudsocq F., Woodgate R., Yang W. Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass replication. Cell. 107:2001;91-102 The crystal structures of Dpo4-DNA complexes revealed the details of protein-DNA interactions and a mechanism by which the Y-family polymerases perform low-fidelity and translesion DNA synthesis.
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Cell
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Ling, H.1
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41
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0035862988
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Domain structure, localization, and function of DNA polymerase η, defective in xeroderma pigmentosum variant cells
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Kannouche P., Broughton B.C., Volker M., Hanaoka F., Mullenders L.H., Lehmann A.R. Domain structure, localization, and function of DNA polymerase η, defective in xeroderma pigmentosum variant cells. Genes Dev. 15:2001;158-172.
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42
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0034852569
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Interaction with PCNA is essential for yeast DNA polymerase η function
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This paper reports the role of PCNA in lesion-bypass DNA synthesis and identifies the region of Pol η that interacts physically with PCNA.
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Haracska L., Kondratick C.M., Unk I., Prakash S., Prakash L. Interaction with PCNA is essential for yeast DNA polymerase η function. Mol. Cell. 8:2001;407-415 This paper reports the role of PCNA in lesion-bypass DNA synthesis and identifies the region of Pol η that interacts physically with PCNA.
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Haracska, L.1
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43
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0035966270
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Yeast DNA polymerase η utilizes an induced-fit mechanism of nucleotide incorporation
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Mutations in human DNA polymerase η motif II alter bypass of DNA lesions
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Glick E., Vigna K.L., Loeb L.A. Mutations in human DNA polymerase η motif II alter bypass of DNA lesions. EMBO J. 20:2001;7303-7312.
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Two distinct modes of RecA action are required for DNA polymerase V-catalyzed translesion synthesis
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Pham P., Seitz E.M., Saveliev S., Shen X., Woodgate R., Cox M.M., Goodman M.F. Two distinct modes of RecA action are required for DNA polymerase V-catalyzed translesion synthesis. Proc. Natl. Acad. Sci. USA. 99:2002;11061-11066.
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Pham, P.1
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Lesion bypass by the Escherichia coli DNA polymerase V requires assembly of a RecA nucleoprotein filament
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Reuven N.B., Arad G., Stasiak A.Z., Stasiak A., Livneh Z. Lesion bypass by the Escherichia coli DNA polymerase V requires assembly of a RecA nucleoprotein filament. J. Biol. Chem. 276:2001;5511-5517.
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The processivity factor β controls DNA polymerase IV traffic during spontaneous mutagenesis and translesion synthesis in vivo
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This paper provides a connection between regular DNA synthesis and translesion synthesis in bacteria, which is through β clamp, the processivity factor (PCNA equivalent).
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Lenne-Samuel N., Wagner J., Etienne H., Fuchs R.P. The processivity factor β controls DNA polymerase IV traffic during spontaneous mutagenesis and translesion synthesis in vivo. EMBO Rep. 3:2002;45-49 This paper provides a connection between regular DNA synthesis and translesion synthesis in bacteria, which is through β clamp, the processivity factor (PCNA equivalent).
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Synthetic activity of Sso DNA polymerase Y1, an archaeal DinB-like DNA polymerase, is stimulated by processivity factors proliferating cell nuclear antigen and replication factor C
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Gruz P., Pisani F.M., Shimizu M., Yamada M., Hayashi I., Morikawa K., Nohmi T. Synthetic activity of Sso DNA polymerase Y1, an archaeal DinB-like DNA polymerase, is stimulated by processivity factors proliferating cell nuclear antigen and replication factor C. J. Biol. Chem. 276:2001;47394-47401.
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Requirement of RAD5 and MMS2 for postreplication repair of UV-damaged DNA in Saccharomyces cerevisiae
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Torres-Ramos C.A., Prakash S., Prakash L. Requirement of RAD5 and MMS2 for postreplication repair of UV-damaged DNA in Saccharomyces cerevisiae. Mol. Cell Biol. 22:2002;2419-2426.
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50
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RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
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This paper identifies for the first time the sites of ubiquitination and sumoylation on yeast and human PCNA and the correlation between these modifications and DNA repair.
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Hoege C., Pfander B., Moldovan G.L., Pyrowolakis G., Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature. 419:2002;135-141 This paper identifies for the first time the sites of ubiquitination and sumoylation on yeast and human PCNA and the correlation between these modifications and DNA repair.
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Hoege, C.1
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Ribbon models of macromolecules
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Carson M. Ribbon models of macromolecules. J. Mol. Graph. 5:1987;103-106.
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