Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 100, Issue 23, Pages 13219-13224Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.2235804100
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Funding
- NIAID NIH HHS [R01 AI016892, AI-16892] Funding Source: Medline
- NIGMS NIH HHS [R01 GM049224-10, R01 GM049224, GM-499224] Funding Source: Medline
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The Escherichia coli UmuD' protein is a component of DNA polymerase V, an error-prone polymerase that carries out translesion synthesis on damaged DNA templates. The intracellular concentration of UmuD' is strictly controlled by regulated transcription, by posttranslational processing of UmuD to UmuD', and by ClpXP degradation. UmuD' is a substrate for the ClpXP protease but must form a heterodimer with its unabbreviated precursor, UmuD, for efficient degradation to occur. Here,we show that UmuD functions as a UmuD' delivery protein for ClpXP. UmuD can also deliver a UmuD partner for degradation. UmuD resembles SspB, a well-characterized substrate-delivery protein for ClpX, in that both proteins use related peptide motifs to bind to the N-terminal domain of ClpX, thereby tethering substrate complexes to ClpXP. The combined use of a weak substrate recognition signal and a delivery factor that tethers the substrate to the protease allows regulated proteolysis of UmuD/D' in the cell. Dual recognition strategies of this type may be a relatively common feature of intracellular protein turnover.
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