DNA Polymerase: Structural Homology, Conformational Dynamics, and the Effects of Carcinogenic DNA Adducts
DNA replication is vital for an organism to proliferate and lying at the heart of this process is the enzyme DNA polymerase. Most DNA polymerases have a similar three dimensional fold, akin to a human right hand, despite differences in sequence homology. This structural homology would predict a rela...
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| Format: | Article |
| Language: | English |
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Wiley
2010-01-01
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| Series: | Journal of Nucleic Acids |
| Online Access: | http://dx.doi.org/10.4061/2010/457176 |
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| _version_ | 1832564196915544064 |
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| author | Richard G. Federley Louis J. Romano |
| author_facet | Richard G. Federley Louis J. Romano |
| author_sort | Richard G. Federley |
| collection | DOAJ |
| description | DNA replication is vital for an organism to proliferate and lying at the heart of this process is the enzyme
DNA polymerase. Most DNA polymerases have a similar three dimensional fold, akin to a human right
hand, despite differences in sequence homology. This structural homology would predict a relatively
unvarying mechanism for DNA synthesis yet various polymerases exhibit markedly different properties
on similar substrates, indicative of each type of polymerase being prescribed to a specific role in DNA
replication. Several key conformational steps, discrete states, and structural moieties have been
identified that contribute to the array of properties the polymerases exhibit. The ability of carcinogenic
adducts to interfere with conformational processes by directly interacting with the protein explicates
the mutagenic consequences these adducts impose. Recent studies have identified novel states that
have been hypothesised to test the fit of the nascent base pair, and have also shown the enzyme to
possess a lively quality by continually sampling various conformations. This review focuses on the
homologous structural changes that take place in various DNA polymerases, both replicative and those
involved in adduct bypass, the role these changes play in selection of a correct substrate, and how the
presence of bulky carcinogenic adducts affects these changes. |
| format | Article |
| id | doaj-art-5e0aaca27c93489d8f3d5f021655490d |
| institution | Kabale University |
| issn | 2090-021X |
| language | English |
| publishDate | 2010-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Journal of Nucleic Acids |
| spelling | doaj-art-5e0aaca27c93489d8f3d5f021655490d2025-02-03T01:11:39ZengWileyJournal of Nucleic Acids2090-021X2010-01-01201010.4061/2010/457176457176DNA Polymerase: Structural Homology, Conformational Dynamics, and the Effects of Carcinogenic DNA AdductsRichard G. Federley0Louis J. Romano1Department of Chemistry, Wayne State University, Detroit, MI 48202, USADepartment of Chemistry, Wayne State University, Detroit, MI 48202, USADNA replication is vital for an organism to proliferate and lying at the heart of this process is the enzyme DNA polymerase. Most DNA polymerases have a similar three dimensional fold, akin to a human right hand, despite differences in sequence homology. This structural homology would predict a relatively unvarying mechanism for DNA synthesis yet various polymerases exhibit markedly different properties on similar substrates, indicative of each type of polymerase being prescribed to a specific role in DNA replication. Several key conformational steps, discrete states, and structural moieties have been identified that contribute to the array of properties the polymerases exhibit. The ability of carcinogenic adducts to interfere with conformational processes by directly interacting with the protein explicates the mutagenic consequences these adducts impose. Recent studies have identified novel states that have been hypothesised to test the fit of the nascent base pair, and have also shown the enzyme to possess a lively quality by continually sampling various conformations. This review focuses on the homologous structural changes that take place in various DNA polymerases, both replicative and those involved in adduct bypass, the role these changes play in selection of a correct substrate, and how the presence of bulky carcinogenic adducts affects these changes.http://dx.doi.org/10.4061/2010/457176 |
| spellingShingle | Richard G. Federley Louis J. Romano DNA Polymerase: Structural Homology, Conformational Dynamics, and the Effects of Carcinogenic DNA Adducts Journal of Nucleic Acids |
| title | DNA Polymerase: Structural Homology, Conformational Dynamics, and the Effects of Carcinogenic DNA Adducts |
| title_full | DNA Polymerase: Structural Homology, Conformational Dynamics, and the Effects of Carcinogenic DNA Adducts |
| title_fullStr | DNA Polymerase: Structural Homology, Conformational Dynamics, and the Effects of Carcinogenic DNA Adducts |
| title_full_unstemmed | DNA Polymerase: Structural Homology, Conformational Dynamics, and the Effects of Carcinogenic DNA Adducts |
| title_short | DNA Polymerase: Structural Homology, Conformational Dynamics, and the Effects of Carcinogenic DNA Adducts |
| title_sort | dna polymerase structural homology conformational dynamics and the effects of carcinogenic dna adducts |
| url | http://dx.doi.org/10.4061/2010/457176 |
| work_keys_str_mv | AT richardgfederley dnapolymerasestructuralhomologyconformationaldynamicsandtheeffectsofcarcinogenicdnaadducts AT louisjromano dnapolymerasestructuralhomologyconformationaldynamicsandtheeffectsofcarcinogenicdnaadducts |