Reachability in Two-Clock Timed Automata is PSPACE-complete

Recently, Haase, Ouaknine, and Worrell have shown that reachability in two-clock timed automata is log-space equivalent to reachability in bounded one-counter automata. We show that reachability in bounded one-counter automata is PSPACE-complete

New Deterministic Algorithms for Solving Parity Games

We study parity games in which one of the two players controls only a small number $k$ of nodes and the other player controls the $n-k$ other nodes of the game. Our main result is a fixed-parameter algorithm that solves bipartite parity games in time $k^{O(\sqrt{k})}\cdot O(n^3)$, and general parity games in time $(p+k)^{O(\sqrt{k})} \cdot O(pnm)$, where $p$ is the number of distinct priorities and $m$ is the number of edges. For all games with $k = o(n)$ this improves the previously fastest algorithm by Jurdzi{\'n}ski, Paterson, and Zwick (SICOMP 2008). We also obtain novel kernelization results and an improved deterministic algorithm for graphs with small average degree

Symmetric Strategy Improvement

Symmetry is inherent in the definition of most of the two-player zero-sum games, including parity, mean-payoff, and discounted-payoff games. It is therefore quite surprising that no symmetric analysis techniques for these games exist. We develop a novel symmetric strategy improvement algorithm where, in each iteration, the strategies of both players are improved simultaneously. We show that symmetric strategy improvement defies Friedmann's traps, which shook the belief in the potential of classic strategy improvement to be polynomial

The Electronic and Superconducting Properties of Oxygen-Ordered MgB2 compounds of the form Mg2B3Ox

Possible candidates for the Mg2B3Ox nanostructures observed in bulk of polycrystalline MgB2 (Ref.1) have been studied using a combination of Z-contrast imaging, electron energy loss spectroscopy (EELS) and first-principles calculations. The electronic structures, phonon modes, and electron phonon coupling parameters are calculated for two oxygen-ordered MgB2 compounds of composition Mg2B3O and Mg2B3O2, and compared with those of MgB2. We find that the density of states for both Mg2B3Ox structures show very good agreement with EELS, indicating that they are excellent candidates to explain the observed coherent oxygen precipitates. Incorporation of oxygen reduces the transition temperature and gives calculated TC values of 18.3 K and 1.6 K for Mg2B3O and Mg2B3O2, respectively.Comment: Submitted to PR

Complementary DNA sequences of two 14.5 kDa subunits of NADH:ubiquinone oxidoreductase from bovine heart mitochondria Completion of the primary structure of the complex?

AbstractThe amino acid sequences of two nuclear-encoded subunits of complex I from bovine heart mitochondria have been determined. Both proteins have an apparent molecular weight of 14.5 kDa and their N-α-amino groups are acetylated. They are known as subunits B14.5a and B14.5b. Neither protein is evidently related to any known protein and their functions are obscure. A total of 34 nuclear-encoded subunits of bovine complex 1 have now been sequenced and it is thought that the primary structure of the complex is now complete, although with such a complicated structure it is difficult to be certain that there are no other subunits remaining to be sequenced. Seven additional hydrophobic subunits of the enzyme are encoded in mitochondrial DNA, and therefore bovine heart complex I is an assembly of about 41 different proteins. If it is assumed that there is one copy of each protein in the assembly, these polypeptides contain 7,955 amino acids in their sequences, more than are found in the Escherichia coli ribosome, which contains 7,336 amino acids in its 32 polypeptides

Identification in Saccharomyces cerevisiae of two isoforms of a novel mitochondrial transporter for 2-oxoadipate and 2-oxoglutarate.

The nuclear genome of Saccharomyces cerevisiae encodes 35 members of a family of membrane proteins. Known members transport substrates and products across the inner membranes of mitochondria. We have localized two hitherto unidentified family members, Odc1p and Odc2p, to the inner membranes of mitochondria. They are isoforms with 61% sequence identity, and we have shown in reconstituted liposomes that they transport the oxodicarboxylates 2-oxoadipate and 2-oxoglutarate by a strict counter exchange mechanism. Intraliposomal adipate and glutarate and to a lesser extent malate and citrate supported [14C]oxoglutarate uptake. The expression of Odc1p, the more abundant isoform, made in the presence of nonfermentable carbon sources, is repressed by glucose. The main physiological roles of Odc1p and Odc2p are probably to supply 2-oxoadipate and 2-oxoglutarate from the mitochondrial matrix to the cytosol where they are used in the biosynthesis of lysine and glutamate, respectively, and in lysine catabolism

The affinity purification and characterization of ATP synthase complexes from mitochondria.

The mitochondrial F₁-ATPase inhibitor protein, IF₁, inhibits the hydrolytic, but not the synthetic activity of the F-ATP synthase, and requires the hydrolysis of ATP to form the inhibited complex. In this complex, the α-helical inhibitory region of the bound IF₁ occupies a deep cleft in one of the three catalytic interfaces of the enzyme. Its N-terminal region penetrates into the central aqueous cavity of the enzyme and interacts with the γ-subunit in the enzyme's rotor. The intricacy of forming this complex and the binding mode of the inhibitor endow IF₁ with high specificity. This property has been exploited in the development of a highly selective affinity procedure for purifying the intact F-ATP synthase complex from mitochondria in a single chromatographic step by using inhibitor proteins with a C-terminal affinity tag. The inhibited complex was recovered with residues 1-60 of bovine IF₁ with a C-terminal green fluorescent protein followed by a His-tag, and the active enzyme with the same inhibitor with a C-terminal glutathione-S-transferase domain. The wide applicability of the procedure has been demonstrated by purifying the enzyme complex from bovine, ovine, porcine and yeast mitochondria. The subunit compositions of these complexes have been characterized. The catalytic properties of the bovine enzyme have been studied in detail. Its hydrolytic activity is sensitive to inhibition by oligomycin, and the enzyme is capable of synthesizing ATP in vesicles in which the proton-motive force is generated from light by bacteriorhodopsin. The coupled enzyme has been compared by limited trypsinolysis with uncoupled enzyme prepared by affinity chromatography. In the uncoupled enzyme, subunits of the enzyme's stator are degraded more rapidly than in the coupled enzyme, indicating that uncoupling involves significant structural changes in the stator region