86 research outputs found

    Protein S-acyl Transferase 15 is Involved in Seed Triacylglycerol Catabolism during Early Seedling Growth in Arabidopsis

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    Seeds of Arabidopsis contain ~40% of triacylglycerol. It is converted to sugar to support post germination growth. We identified an Arabidopsis T-DNA knockout mutant that was sugar dependent during early seedling establishment. Our study showed that the β-oxidation process involved in catabolising the free fatty acids released from the seed triacylglycerol was impaired in this mutant. This mutant was confirmed to be transcriptional null for the Protein Acyl Transferase 15, AtPAT15 (At5g04270), one of the 24 protein acyl transferases in Arabidopsis. Although it is the shortest AtPAT15 contains the signature ‘Asp-His-His-Cys cysteine rich domain’ which is essential for the enzyme activity of this family of proteins. The function of AtPAT15 was validated because it rescued the growth defect of the yeast protein acyl transferase mutant akr1 and it was also auto-acylated in vitro. Transient expression of AtPAT15 in Arabidopsis and tobacco localized AtPAT15 in the Golgi apparatus. Taken together, our data clearly demonstrated that AtPAT15 is involved in β-oxidation of triacylglycerol, revealing the importance of protein S-acylation in seed storage lipid breakdown during early seedling growth of Arabidopsis

    Photoinduced charge separation in Q1D heterojunction materials: Evidence for electron-hole pair separation in mixed-halide MXMX solids

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    Resonance Raman experiments on doped and photoexcited single crystals of mixed-halide MXMX complexes (MM=Pt; XX=Cl,Br) clearly indicate charge separation: electron polarons preferentially locate on PtBr segments while hole polarons are trapped within PtCl segments. This polaron selectivity, potentially very useful for device applications, is demonstrated theoretically using a discrete, 3/4-filled, two-band, tight-binding, extended Peierls-Hubbard model. Strong hybridization of the PtCl and PtBr electronic bands is the driving force for separation.Comment: n LaTeX, figures available by mail from JTG ([email protected]

    Excitation Spectrum of One-dimensional Extended Ionic Hubbard Model

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    We use Perturbative Continuous Unitary Transformations (PCUT) to study the one dimensional Extended Ionic Hubbard Model (EIHM) at half-filling in the band insulator region. The extended ionic Hubbard model, in addition to the usual ionic Hubbard model, includes an inter-site nearest-neighbor (n.n.) repulsion, VV. We consider the ionic potential as unperturbed part of the Hamiltonian, while the hopping and interaction (quartic) terms are treated as perturbation. We calculate total energy and ionicity in the ground state. Above the ground state, (i) we calculate the single particle excitation spectrum by adding an electron or a hole to the system. (ii) the coherence-length and spectrum of electron-hole excitation are obtained. Our calculations reveal that for V=0, there are two triplet bound state modes and three singlet modes, two anti-bound states and one bound state, while for finite values of VV there are four excitonic bound states corresponding to two singlet and two triplet modes. The major role of on-site Coulomb repulsion UU is to split singlet and triplet collective excitation branches, while VV tends to pull the singlet branches below the continuum to make them bound states.Comment: 10 eps figure

    Signatures of Stripe Phases in Hole Doped La2NiO4La_2NiO_4

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    We study nickelate-centered and oxygen-centered stripe phases in doped La2_{2}NiO4_{4} materials. We use an inhomogeneous Hartree-Fock and random-phase approximation approach including both electron-electron and electron-lattice(e-l) coupling for a layer of La2_{2}NiO4_{4}. We find that whether the ground state after commensurate hole doping comprises Ni-centered or O-centered charge-localized stripes depends sensitively on the e-l interaction. With increasing e-l interaction strength, a continuous transition from an O-centered stripe phase to a Ni-centered one is found. Various low- and high-energy signatures of these two kinds of stripe phases are predicted, which can clearly distinguish them. These signatures reflect the strongly correlated spin-charge-lattice features in the vicinity of Ni-centered or O-centered stripe domains. The importance of e-l interaction for recent experiments on stripe phases is discussed.Comment: 11 pages, 12 figures, to appear in Phys.Rev.B(July 1,1998

    Pressure Tuning of the Charge Density Wave in the Halogen-Bridged Transition-Metal (MX) Solid Pt2Br6(NH3)4Pt_2Br_6(NH_3)_4

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    We report the pressure dependence up to 95 kbar of Raman active stretching modes in the quasi-one-dimensional MX chain solid Pt2Br6(NH3)4Pt_2Br_6(NH_3)_4. The data indicate that a predicted pressure-induced insulator-to-metal transition does not occur, but are consistent with the solid undergoing either a three-dimensional structural distortion, or a transition from a charge-density wave to another broken-symmetry ground state. We show that such a transition cacan be well-modeled within a Peierls-Hubbard Hamiltonian. 1993 PACS: 71.30.+h, 71.45.Lr, 75.30.Fv, 78.30.-j, 81.40.VwComment: 4 pages, ReVTeX 3.0, figures available from the authors on request (Gary Kanner, [email protected]), to be published in Phys Rev B Rapid Commun, REVISION: minor typos corrected, LA-UR-94-246

    Identification of Giardia lamblia DHHC Proteins and the Role of Protein S-palmitoylation in the Encystation Process

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    Protein S-palmitoylation, a hydrophobic post-translational modification, is performed by protein acyltransferases that have a common DHHC Cys-rich domain (DHHC proteins), and provides a regulatory switch for protein membrane association. In this work, we analyzed the presence of DHHC proteins in the protozoa parasite Giardia lamblia and the function of the reversible S-palmitoylation of proteins during parasite differentiation into cyst. Two specific events were observed: encysting cells displayed a larger amount of palmitoylated proteins, and parasites treated with palmitoylation inhibitors produced a reduced number of mature cysts. With bioinformatics tools, we found nine DHHC proteins, potential protein acyltransferases, in the Giardia proteome. These proteins displayed a conserved structure when compared to different organisms and are distributed in different monophyletic clades. Although all Giardia DHHC proteins were found to be present in trophozoites and encysting cells, these proteins showed a different intracellular localization in trophozoites and seemed to be differently involved in the encystation process when they were overexpressed. dhhc transgenic parasites showed a different pattern of cyst wall protein expression and yielded different amounts of mature cysts when they were induced to encyst. Our findings disclosed some important issues regarding the role of DHHC proteins and palmitoylation during Giardia encystation.Fil: Merino, Maria Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; ArgentinaFil: Zamponi, Nahuel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; ArgentinaFil: Vranych, Cecilia Verónica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; ArgentinaFil: Touz, Maria Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; ArgentinaFil: Ropolo, Andrea Silvana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentin
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