The Roles of UmuD in Regulating Mutagenesis
All organisms are subject to DNA damage from both endogenous and environmental sources. DNA damage that is not fully repaired can lead to mutations. Mutagenesis is now understood to be an active process, i...
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| Main Authors: | , , |
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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/10.4061/2010/947680 |
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| author | Jaylene N. Ollivierre Jing Fang Penny J. Beuning |
| author_facet | Jaylene N. Ollivierre Jing Fang Penny J. Beuning |
| author_sort | Jaylene N. Ollivierre |
| collection | DOAJ |
| description | All organisms are
subject to DNA damage from both endogenous and
environmental sources. DNA damage that is not
fully repaired can lead to mutations.
Mutagenesis is now understood to be an active
process, in part facilitated by lower-fidelity
DNA polymerases that replicate DNA in an
error-prone manner. Y-family DNA polymerases,
found throughout all domains of life, are
characterized by their lower fidelity on
undamaged DNA and their specialized ability to
copy damaged DNA. Two E. coli Y-family DNA polymerases are responsible for
copying damaged DNA as well as for mutagenesis.
These DNA polymerases interact with different
forms of UmuD, a dynamic protein that regulates
mutagenesis. The UmuD gene
products, regulated by the SOS response, exist
in two principal forms: UmuD2, which prevents mutagenesis, and UmuD2′, which facilitates UV-induced mutagenesis. This paper focuses on the multiple conformations of the UmuD gene products and how their protein interactions regulate mutagenesis. |
| format | Article |
| id | doaj-art-20ab9724579446158b1040920a2284f8 |
| 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-20ab9724579446158b1040920a2284f82025-02-03T01:20:33ZengWileyJournal of Nucleic Acids2090-021X2010-01-01201010.4061/2010/947680947680The Roles of UmuD in Regulating MutagenesisJaylene N. Ollivierre0Jing Fang1Penny J. Beuning2Department of Chemistry and Chemical Biology, Northeastern University, 360 Huntington Avenue, 102 Hurtig Hall, Boston, MA 02115, USADepartment of Chemistry and Chemical Biology, Northeastern University, 360 Huntington Avenue, 102 Hurtig Hall, Boston, MA 02115, USADepartment of Chemistry and Chemical Biology, Northeastern University, 360 Huntington Avenue, 102 Hurtig Hall, Boston, MA 02115, USAAll organisms are subject to DNA damage from both endogenous and environmental sources. DNA damage that is not fully repaired can lead to mutations. Mutagenesis is now understood to be an active process, in part facilitated by lower-fidelity DNA polymerases that replicate DNA in an error-prone manner. Y-family DNA polymerases, found throughout all domains of life, are characterized by their lower fidelity on undamaged DNA and their specialized ability to copy damaged DNA. Two E. coli Y-family DNA polymerases are responsible for copying damaged DNA as well as for mutagenesis. These DNA polymerases interact with different forms of UmuD, a dynamic protein that regulates mutagenesis. The UmuD gene products, regulated by the SOS response, exist in two principal forms: UmuD2, which prevents mutagenesis, and UmuD2′, which facilitates UV-induced mutagenesis. This paper focuses on the multiple conformations of the UmuD gene products and how their protein interactions regulate mutagenesis.http://dx.doi.org/10.4061/2010/947680 |
| spellingShingle | Jaylene N. Ollivierre Jing Fang Penny J. Beuning The Roles of UmuD in Regulating Mutagenesis Journal of Nucleic Acids |
| title | The Roles of UmuD in Regulating Mutagenesis |
| title_full | The Roles of UmuD in Regulating Mutagenesis |
| title_fullStr | The Roles of UmuD in Regulating Mutagenesis |
| title_full_unstemmed | The Roles of UmuD in Regulating Mutagenesis |
| title_short | The Roles of UmuD in Regulating Mutagenesis |
| title_sort | roles of umud in regulating mutagenesis |
| url | http://dx.doi.org/10.4061/2010/947680 |
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