Inhibition of yeast ribonucleotide reductase by Sml1 depends on the allosteric state of the enzyme.
Sml1 is an intrinsically disordered protein inhibitor of Saccharomyces cerevisiae ribonucleotide reductase (ScRR1), but its inhibition is poorly understood. RR reduces ribonucleoside diphosphates to their deoxy forms, and balances the nucleotide pool. Multiple turnover kinetics show that Sml1 inhibition of dGTP/ADP and ATP/CDP bound ScRR follows a mixed inhibition mechanism. ... However, Sml1 cooperatively binds to the ES complex in the dGTP/ADP form, whereas with ATP/CDP, Sml1 binds weakly and non-cooperatively. Gel filtration and mutagenesis studies indicate that Sml1 doesn't alter the multimerization equilibrium and the CXXC motif is not involved in the inhibition. The data suggest that Sml1 is an allosteric inhibitor. This article is protected by copyright. All rights reserved.
FEBS Lett.
Date: May. 07, 2016
PubMed ID: 27155231
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