umuD Antibody

1. 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) PMID: 27236212
2. 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 PMID: 25811184
3. Like the self-cleaving serine proteases LexA and UmuD in Escherichia coli, UmuDAb required RecA for cleavage. PMID: 22697494
4. 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 PMID: 21975937
5. 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. PMID: 21784925
6. 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. PMID: 21118802
7. REVIEW: properties and functions of Pol V PMID: 15588845
8. 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. PMID: 16199565
9. Lyase activity intrinsic to polymerase V PMID: 16202661
10. AlkB dioxygenase, PolV (UmuD'C), and AlkA have roles in preventing MMS-induced mutagenesis in Escherichia coli PMID: 16226494
11. found new class of UmuD variant proteins that fail to undergo cleavage but whose properties resemble those of the cleaved version, UmuD' PMID: 16464848
12. 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. PMID: 18216271

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KEGG: ecj:JW1172

STRING: 511145.b1183