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EC Number
Posttranslational Modification
Commentary
Reference
proteolytic modification
inactive form UmuD is cleaved into active form UmuD'
proteolytic modification
inactive UmuD is posttranslationally activated by a RecA-mediated cleavage at its Gys24-Gly25 bond that yields UmuD', UmuD monomer is a better substrate for the cleavage reaction than the dimer
proteolytic modification
inactive UmuD is posttranslationally activated by a RecA-mediated cleavage that yields UmuD'
proteolytic modification
inactive UmuD is posttranslationally activated by a RecA-mediated cleavage that yields UmuD', P67D and P67R mutations of RecA result in reduced UmuD cleavage
proteolytic modification
processing of UmuD to the shorter, but mutagenically active UmuD' by activated RecA
proteolytic modification
processing of UmuD to the shorter, but mutagenically active UmuD' by ClpXP protease, UmuD' must form a heterodimer with its unabbreviated precursor for efficient degradation, UmuD2 homodimers are degraded with an efficiency similar to the UmuD' subunit of the UmuD/UmuD' heterodimer
proteolytic modification
RecA-facilitated cleavage of UmuD to UmuD' can be inhibited by overexpression of polymerase III subunits that interact with UmuD
proteolytic modification
RecA-facilitated cleavage of UmuD yields a carboxy-terminal fragment UmuD' that is active for mutagenesis, no other SOS gene products other than activated RecA are required for UmuD processing, high levels of activated RecA are required for cleavage in vivo
proteolytic modification
RecA-mediated posttranslational processing of UmuD to the shorter, but mutagenically active UmuD'
proteolytic modification
RecA-mediated posttranslational processing of UmuD to the shorter, but mutagenically active UmuD', K232A/E235A mutant of RecA cleaves UmuD more efficiently than wild-type RecA, T242A/R234A mutant of RecA is defective for cleavage of UmuD
Results 1 - 10 of 15 > >>