PMID:21118802
| Citation |
Ollivierre, JN, Sikora, JL and Beuning, PJ (2011) The dimeric SOS mutagenesis protein UmuD is active as a monomer. J. Biol. Chem. 286:3607-17 |
|---|---|
| Abstract |
The homodimeric umuD gene products play key roles in regulating the cellular response to DNA damage in Escherichia coli. UmuD(2) is composed of 139-amino acid subunits and is up-regulated as part of the SOS response. Subsequently, damage-induced RecA·ssDNA nucleoprotein filaments mediate the slow self-cleavage of the N-terminal 24-amino acid arms yielding UmuD'(2). UmuD(2) and UmuD'(2) make a number of distinct protein-protein contacts that both prevent and facilitate mutagenic translesion synthesis. 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 UmuD N41D monomer is proficient for cleavage and interacts physically with DNA polymerase IV (DinB) and the β clamp. Furthermore, the N41D variants facilitate UV-induced mutagenesis and promote overall cell viability. Taken together, these observations show that a monomeric form of UmuD retains substantial function in vivo and in vitro. |
| Links |
PubMed PMC3030365 Online version:10.1074/jbc.M110.167254 |
| Keywords |
Amino Acid Substitution; Cell Survival; DNA-Directed DNA Polymerase/genetics; DNA-Directed DNA Polymerase/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Mutagenesis/radiation effects; Mutant Proteins/chemistry; Mutant Proteins/metabolism; Protein Multimerization; Protein Stability; SOS Response (Genetics) |
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