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1,10-phenanthroline inhibits sumoylation and reveals that yeast SUMO modifications are highly transient

ABSTRACT: The steady state levels of protein sumoylation depend on relative rates of conjugation and desumoylation. Whether SUMO modifications are generally long-lasting or short-lived is unknown. Here we show that treating budding yeast cultures with 1,10-phenanthroline abolishes most SUMO conjugations within one minute, without impacting ubiquitination, an analogous post-translational modification. 1,10-phenanthroline inhibits formation of the E1~SUMO thioester intermediate, demonstrating that it targets the first step in the sumoylation pathway. SUMO conjugations are retained after treatment with 1,10-phenanthroline in yeast that express a defective form of the desumoylase Ulp1, indicating that Ulp1 is responsible for eliminating existing SUMO modifications almost instantly, when de novo sumoylation is inhibited. This reveals that SUMO modifications are normally extremely transient because of continuous desumoylation by Ulp1. Supporting our findings, we demonstrate that sumoylation of two specific targets, Sko1 and Tfg1, virtually disappears within one minute of impairing de novo sumoylation. Altogether, we have identified an extremely rapid and potent inhibitor of sumoylation, and our work reveals that SUMO modifications are remarkably short-lived.

SUBMITTER: J., Bryan McNeil

PROVIDER: S-SCDT-10_1038-S44319-023-00010-8 | biostudies-other |

REPOSITORIES: biostudies-other

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1,10-phenanthroline inhibits sumoylation and reveals that yeast SUMO modifications are highly transient.

Project description:The steady-state levels of protein sumoylation depend on relative rates of conjugation and desumoylation. Whether SUMO modifications are generally long-lasting or short-lived is unknown. Here we show that treating budding yeast cultures with 1,10-phenanthroline abolishes most SUMO conjugations within one minute, without impacting ubiquitination, an analogous post-translational modification. 1,10-phenanthroline inhibits the formation of the E1~SUMO thioester intermediate, demonstrating that it targets the first step in the sumoylation pathway. SUMO conjugations are retained after treatment with 1,10-phenanthroline in yeast that express a defective form of the desumoylase Ulp1, indicating that Ulp1 is responsible for eliminating existing SUMO modifications almost instantly when de novo sumoylation is inhibited. This reveals that SUMO modifications are normally extremely transient because of continuous desumoylation by Ulp1. Supporting our findings, we demonstrate that sumoylation of two specific targets, Sko1 and Tfg1, virtually disappears within one minute of impairing de novo sumoylation. Altogether, we have identified an extremely rapid and potent inhibitor of sumoylation, and our work reveals that SUMO modifications are remarkably short-lived.

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Project description:In the title compound, [Mg(C(12)H(8)N(2))(2)(H(2)O)(2)][Cr(2)O(7)]·2C(12)H(8)N(2), the cation and anion are situated on a twofold rotation axis. The Mg(II) ion is coordinated by four N atoms from two 1,10-phenanthroline ligands and two O atoms from coordinated water mol-ecules in a distorted octa-hedral geometry. Inter-molecular O-H⋯N and O-H⋯O hydrogen bonds and π-π inter-actions between the aromatic rings [shortest centroid-centroid separation = 3.527 (2) Å] link the cations, anions and 1,10-phenanthroline solvent mol-ecules into a hydrogen-bonded cluster.

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Ligands with 1,10-phenanthroline scaffold for highly regioselective iron-catalyzed alkene hydrosilylation.

Project description:Transition-metal-catalyzed alkene hydrosilylation is one of the most important homogeneous catalytic reactions, and the development of methods that use base metals, especially iron, as catalysts for this transformation is a growing area of research. However, the limited number of ligand scaffolds applicable for base-metal-catalyzed alkene hydrosilylation has seriously hindered advances in this area. Herein, we report the use of 1,10-phenanthroline ligands in base-metal catalysts for alkene hydrosilylation. In particular, iron catalysts with 2,9-diaryl-1,10-phenanthroline ligands exhibit unexpected reactivity and selectivity for hydrosilylation of alkenes, including unique benzylic selectivity with internal alkenes, Markovnikov selectivity with terminal styrenes and 1,3-dienes, and excellent activity toward aliphatic terminal alkenes. According to the mechanistic studies, the unusual benzylic selectivity of this hydrosilylation initiates from ?-? interaction between the phenyl of the alkene and the phenanthroline of the ligand. This ligand scaffold and its unique catalytic model will open possibilities for base-metal-catalyzed hydrosilylation reactions.

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2,9-Dichloro-1,10-phenanthroline.

Project description:The title mol-ecule, C(12)H(6)Cl(2)N(2), is almost planar (the r.m.s. deviation of C atoms is 0.04 Å). The C-N and C-C distances indicate delocalization of the π-electrons in the aromatic fused-ring system.

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Project description:Elongation of the telomeric overhang by telomerase is counteracted by synthesis of the complementary strand by the CST complex, CTC1(Cdc13)/Stn1/Ten1. Interaction of budding yeast Stn1 with overhang-binding Cdc13 is increased by Cdc13 SUMOylation. Human and fission yeast CST instead interact with overhang-binding TPP1/POT1. We show that the fission yeast TPP1 ortholog, Tpz1, is SUMOylated. Tpz1 SUMOylation restricts telomere elongation and promotes Stn1/Ten1 telomere association, and a SUMO-Tpz1 fusion protein has increased affinity for Stn1. Our data suggest that SUMO inhibits telomerase through stimulation of Stn1/Ten1 action by Tpz1, highlighting the evolutionary conservation of the regulation of CST function by SUMOylation.

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Difluoridodioxido(1,10-phenanthroline)molybdenum(VI).

Project description:The title compound, [MoF(2)O(2)(C(12)H(8)N(2))], has non-crystallographic mirror symmetry. The Mo(VI) atom shows a distorted octa-hedral environment, with the phenanthroline N atoms and the two oxide groups forming the equatorial plane and the F atoms occupying the apical positions. Weak C-H⋯O and C-H⋯F hydrogen-bonding contacts and π-π inter-actions [centroid-centroid distance = 3.662 (1) Å] connect the complex mol-ecules into a three-dimensional supra-molecular framework.

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The reactions of 1,10-phenanthroline with yeast alcohol dehydrogenase.

Project description:Freshly prepared samples of yeast alcohol dehydrogenase (EC 1.1.1.1) were inhibited by 1,10-phenanthroline at pH 7.0 and 0 degrees C in a two-stage process. The first step appeared to be slowly established, but was rendered reversible by removal of reagent or by addition of excess Zn2+ ions. The second step was irreversible and was associated with the dissociation of the tetrameric enzyme. The presence of saturating concentrations of NAD+ or NADH promoted and enhanced inhibition by the slowly established reversible process, but prevented dissociation of the enzyme. For the incubation mixtures containing NAD+, removal of the 1,10-phenanthroline resulted in virtually complete recovery of activity, whereas, for the incubation mixtures containing NADH, removal of the reagent gave only partial re-activation. The presence of NAD+ and pyrazole, or NADH and acetamide, in incubation mixtures with the enzyme gave rise to ternary complexes that gave protection against both forms of inactivation by 1,10-phenanthroline. The results support the view that at least some of the Zn2+ ions associated with yeast alcohol dehydrogenase have a catalytic, as opposed to a purely structural, role.

| S-EPMC1183641 | biostudies-other

1,10-Phenanthroline-5,6-dione ethanol monosolvate.

Project description:In the title compound, C12H6N2O2·C2H5OH, the mol-ecule of the 1,10-phenanthroline-5,6-dione is approximately planar, with a maximum deviation of 0.051?(1)?Å. In the crystal, mol-ecules are linked by O-H?N and weak C-H?O hydrogen bonds, forming supra-molecular chains propagating along [110]. ?-? stacking inter-actions are observed between the pyridine rings of neighbouring chains, the centroid-centroid separations being 3.6226?(11) and 3.7543?(11)?Å.

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1,10-Phenanthroline-dithio-oxamide (2/1).

Project description:The asymmetric unit of the title compound, C(12)H(8)N(2)·0.5C(2)H(4)N(2)S(2), contains one 1,10-phenanthroline mol-ecule and a half-mol-ecule of dithio-oxamide, which lies across a crystallographic inversion center. The 1,10-phenanthroline unit is not strictly planar, with dihedral angles between the central benzene ring and the pyridine rings of 1.42?(10) and 1.40?(10)°. In the crystal structure, two 1,10-phenanthroline mol-ecules are linked together by one dithio-oxamide via inter-molecular N-H?N hydrogen bonds.

| S-EPMC2979584 | biostudies-literature

4,7-Diphenyl-1,10-phenanthroline methanol hemisolvate.

Project description:The asymmetric unit of the title compound, C24H16N2·0.5CH3OH, is comprised of two independent bathophenanthroline mol-ecules (systematic name: 4,7-diphenyl-1,10-phenanthroline) and one methanol mol-ecule. The bathophenanthroline mol-ecules are not planar as there is a considerable rotation of all terminal phenyl rings with respect to the central phenanthroline units [dihedral angles in the range 52.21 (12)-62.14 (10)°]. In addition, a non-negligible torsion is apparent in one of the phenanthroline units: the angle between the mean planes of the two pyridine rings is 14.84 (13)°. The methanol solvent mol-ecule is linked to both N atoms of a bathophenanthroline mol-ecule through a bifurcated O-H⋯(N,N) hydrogen bond.

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