| Tracking Escherichia coli DNA polymerase V to the entire genome during the SOS response. | Tracking Escherichia coli DNA polymerase V to the entire genome during the SOS response.
Faraz M, Woodgate R, Clausen AR., Free PMC Article | 08/14/2021 |
| Single-molecule fluorescence microscopy reveals modulation of DNA polymerase IV-binding lifetimes by UmuD (K97A) and UmuD'. | Single-molecule fluorescence microscopy reveals modulation of DNA polymerase IV-binding lifetimes by UmuD (K97A) and UmuD'.
Henrikus SS, van Oijen AM, Robinson A. | 08/7/2021 |
| A Comprehensive View of Translesion Synthesis in Escherichia coli. | A Comprehensive View of Translesion Synthesis in Escherichia coli.
Fujii S, Fuchs RP., Free PMC Article | 05/8/2021 |
| DNA binding and synthesis cannot occur until pol V interacts with a RecA nucleoprotein filament (RecA*) and ATP to form a mutasome complex, pol V Mut = UmuD'2C-RecA-ATP. | Conformational regulation of Escherichia coli DNA polymerase V by RecA and ATP.
Jaszczur MM, Vo DD, Stanciauskas R, Bertram JG, Sikand A, Cox MM, Woodgate R, Mak CH, Pinaud F, Goodman MF., Free PMC Article | 04/20/2019 |
| There are multiple levels of regulation imposed on pol V including transcriptional control, posttranslational modification, targeted proteolysis, activation of the catalytic activity of pol V through protein-protein interactions and the very recently described intracellular spatial regulation of pol V. (Review) | Insights into the complex levels of regulation imposed on Escherichia coli DNA polymerase V.
Goodman MF, McDonald JP, Jaszczur MM, Woodgate R., Free PMC Article | 05/20/2017 |
| The current study delves deeper into this process, initiating the task of mapping out the molecular details of the interaction between RecA and UmuD'2C | A RecA protein surface required for activation of DNA polymerase V.
Gruber AJ, Erdem AL, Sabat G, Karata K, Jaszczur MM, Vo DD, Olsen TM, Woodgate R, Goodman MF, Cox MM., Free PMC Article | 01/2/2016 |
| The results suggest that competition between UmuD and ssDNA for DNA polymerase III alpha binding is a new mechanism for polymerase exchange. | Polymerase manager protein UmuD directly regulates Escherichia coli DNA polymerase III α binding to ssDNA.
Chaurasiya KR, Ruslie C, Silva MC, Voortman L, Nevin P, Lone S, Beuning PJ, Williams MC., Free PMC Article | 01/4/2014 |
| Like the self-cleaving serine proteases LexA and UmuD in Escherichia coli, UmuDAb required RecA for cleavage. | The Acinetobacter regulatory UmuDAb protein cleaves in response to DNA damage with chimeric LexA/UmuD characteristics.
Hare JM, Adhikari S, Lambert KV, Hare AE, Grice AN., Free PMC Article | 07/6/2013 |
| Authors propose that the interaction between DNA polymerase III alpha and UmuD contributes to the transition between replicative and translesion synthesis polymerases by removing DNA polymerase III alpha from the beta clamp. | Selective disruption of the DNA polymerase III α-β complex by the umuD gene products.
Silva MC, Nevin P, Ronayne EA, Beuning PJ., Free PMC Article | 10/6/2012 |
| Electron paramagnetic resonance (EPR) spectroscopy study determined that the arms of UmuD2 display a large degree of motion, are largely unbound from the globular C-terminal domain, and that the free energy of dissociation is 2.1 kJ mol-1 | Electron spin labeling reveals the highly dynamic N-terminal arms of the SOS mutagenesis protein UmuD.
Ollivierre JN, Budil DE, Beuning PJ. | 05/19/2012 |
| Study find that mutations of the N-terminal residues of loop 1, N32, N33, and D34, confer hypersensitivity to UV radiation and to 4-nitroquinoline-N-oxide and significantly reduce Pol V-dependent UV-induced mutagenesis. | Characterization of Escherichia coli UmuC active-site loops identifies variants that confer UV hypersensitivity.
Hawver LA, Gillooly CA, Beuning PJ., Free PMC Article | 11/19/2011 |
| Wild-type UmuD(2) and UmuD'(2) form exceptionally tight dimers in solution; however, we show that the single amino acid change N41D generates stable, active UmuD and UmuD' monomers that functionally mimic the dimeric wild-type proteins. | The dimeric SOS mutagenesis protein UmuD is active as a monomer.
Ollivierre JN, Sikora JL, Beuning PJ., Free PMC Article | 03/26/2011 |
| Structural characteristics of relatively poorly understood, intrinsically disordered umuD small dimeric proteins provide a model for the regulation of diverse aspects of the bacterial SOS response. | Regulation of Escherichia coli SOS mutagenesis by dimeric intrinsically disordered umuD gene products.
Simon SM, Sousa FJ, Mohana-Borges R, Walker GC., Free PMC Article | 01/21/2010 |
| Observations indicate that proteins like RecA and UmuD(2) may be responsible for managing the mutagenic potential of DinB orthologs throughout evolution. | UmuD and RecA directly modulate the mutagenic potential of the Y family DNA polymerase DinB.
Godoy VG, Jarosz DF, Simon SM, Abyzov A, Ilyin V, Walker GC., Free PMC Article | 01/21/2010 |
| REVIEW: properties and functions of Pol V | Properties and functions of Escherichia coli: Pol IV and Pol V.
Fuchs RP, Fujii S, Wagner J. | 01/21/2010 |
| AlkB dioxygenase, PolV (UmuD'C), and AlkA have roles in preventing MMS-induced mutagenesis in Escherichia coli | AlkB dioxygenase in preventing MMS-induced mutagenesis in Escherichia coli: effect of Pol V and AlkA proteins.
Nieminuszczy J, Sikora A, Wrzesiński M, Janion C, Grzesiuk E. | 01/21/2010 |
| In the absence of repair or when the repair capacity of the cell has been exceeded, translesion synthesis by polymerase V (Pol V) allows DNA synthesis to resume and is required to protect the arrested replication fork from degradation. | Nucleotide excision repair or polymerase V-mediated lesion bypass can act to restore UV-arrested replication forks in Escherichia coli.
Courcelle CT, Belle JJ, Courcelle J., Free PMC Article | 01/21/2010 |
| found new class of UmuD variant proteins that fail to undergo cleavage but whose properties resemble those of the cleaved version, UmuD' | A non-cleavable UmuD variant that acts as a UmuD' mimic.
Beuning PJ, Simon SM, Zemla A, Barsky D, Walker GC. | 01/21/2010 |
| Lyase activity intrinsic to polymerase V | Lyase activities intrinsic to Escherichia coli polymerases IV and V.
Shen X, Woodgate R, Goodman MF. | 01/21/2010 |