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Literature summary for 3.4.21.B30 extracted from

  • Ollivierre, J.N.; Sikora, J.L.; Beuning, P.J.
    The dimeric SOS mutagenesis protein UmuD is active as a monomer (2011), J. Biol. Chem., 286, 3607-3617.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.B30

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
N41D the mutant generates stable, active UmuD and UmuD’ monomers that functionally mimic the dimeric wild type proteins. The mutant is proficient for cleavage and interacts physically with DNA polymerase IV (DinB) and the beta-clamp, facilitates UV-induced mutagenesis and promotes overall cell viability Escherichia coli
P48G expression of UmuD2 P48G is substantially lower than that of wild type UmuD2 Escherichia coli
V135S/K136A/R139A expression of UmuD2 V135S/K136A/R139A is substantially lower than that of wild type UmuD2 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AG11
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-

Subunits

Subunits Comment Organism
heterodimer UmuD and UmuD’ rapidly form heterodimers in vitro Escherichia coli

Synonyms

Synonyms Comment Organism
UmuD
-
 Escherichia coli

Expression

Organism Comment Expression
Escherichia coli UmuD2 is up-regulated as part of the SOS response up

General Information

General Information Comment Organism
physiological function UmuD regulates the cellular response to DNA damage Escherichia coli