835 research outputs found

    Import of Honeybee Prepromelittin into the Endoplasmic Reticulum

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    Mapping contacts between regulatory domains of skeletal muscle TnC and Tnl by analyses of a single-chain chimeras.

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    The troponin (Tn) complex is formed by TnC, TnI and TnT and is responsible for the calcium-dependent inhibition of muscle contraction. TnC and TnI interact in an antiparallel fashion in which the N domain of TnC binds in a calcium-dependent manner to the C domain of TnI, releasing the inhibitory effect of the latter on the actomyosin interaction. While the crystal structure of the core cardiac muscle troponin complex has been determined, very little high resolution information is available regarding the skeletal muscle TnITnC complex. With the aim of obtaining structural information regarding specific contacts between skeletal muscle TnC and TnI regulatory domains, we have constructed two recombinant chimeric proteins composed of the residues 191 of TnC linked to residues 98182 or 98147 of TnI. The polypeptides were capable of binding to the thin filament in a calcium-dependent manner and to regulate the ATPase reaction of actomyosin. Small angle X-ray scattering results showed that these chimeras fold into compact structures in which the inhibitory plus the C domain of TnI, with the exception of residues 148182, were in close contact with the N-terminal domain of TnC. CD and fluorescence analysis were consistent with the view that the last residues of TnI (148182) are not well folded in the complex. MS analysis of fragments produced by limited trypsinolysis showed that the whole TnC N domain was resistant to proteolysis, both in the presence and in the absence of calcium. On the other hand the TnI inhibitory and C-terminal domains were completely digested by trypsin in the absence of calcium while the addition of calcium results in the protection of only residues 114137

    Effects of phase separation on the magnetization, x-ray diffraction, and Raman scattering of (La1-yNdy)(1-x)CaxMnO3 (y=0,0.5,1.0; x=1/3)

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    Dc-magnetization, x-ray diffraction, and Raman-scattering studies in polycrystalline (La1-yNdy)(t-x)CaxMnO3 (y = 0.0,0.5,1.0, and x = 1/3) samples are presented. The samples with y = 0.5 and 1.0 show complex magnetic states at low temperatures, with a ferromagnetic coupling strength that weal;ens with increasing y. X-ray measurements show a single crystallographic phase at all temperatures for y = 0.5, with lattice parameter anomalies at temperatures related to electronic and magnetic transitions. The presence of high-frequency vibrational modes in Raman-scattering measurements indicates the existence of charge- and orbital-ordered domains for y=0.5 and 1.0, which are closely related to the antiferromagnetic component identified by the magnetization experiments. The close relationship between results obtained by magnetic, structural, and optical probes is discussed.63

    Effects Of Phase Separation On The Magnetization, X-ray Diffraction, And Raman Scattering Of (la1-yndy) 1-xcaxmno3 (y = 0,0.5,1.0;x = 1/3)

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    Dc-magnetization, x-ray diffraction, and Raman-scattering studies in polycrystalline (La1-yNdy)1-xCaxMnO3 (y = 0.0,0.5,1.0, and x = 1/3) samples are presented. The samples with y = 0.5 and 1.0 show complex magnetic states at low temperatures, with a ferromagnetic coupling strength that weakens with increasing y. X-ray measurements show a single crystallographic phase at all temperatures for y=0.5, with lattice parameter anomalies at temperatures related to electronic and magnetic transitions. The presence of high-frequency vibrational modes in Raman-scattering measurements indicates the existence of charge- and orbital-ordered domains for y = 0.5 and 1.0, which are closely related to the antiferromagnetic component identified by the magnetization experiments. The close relationship between results obtained by magnetic, structural, and optical probes is discussed.636644041644046Wollan, E.O., Koehler, W.C., (1955) Phys. Rev., 100, p. 545Goodenough, J.B., (1955) Phys. Rev., 100, p. 564Chen, C.H., Cheong, S.-W., (1996) Phys. Rev. Lett., 76, p. 4042Radaelli, P.G., Cox, D.E., Marezio, M., Cheong, S.-W., Schiffer, P.E., Ramirez, A.P., (1995) Phys. Rev. Lett., 75, p. 4488Hwang, H.Y., Cheong, S.-W., Radaelli, P.G., Marezio, M., Batlogg, B., (1995) Phys. Rev. Lett., 75, p. 914Coey, J.M.D., Viret, M., Ranno, L., Ounadjela, K., (1995) Phys. Rev. Lett., 75, p. 3910Uehara, M., Mori, S., Chen, C.H., Cheong, S.-W., (1999) Nature (London), 399, p. 560Moreo, A., Yunoke, S., Dagotto, E., (1999) Science, 283, p. 2034. , and references thereinArchibald, W., Zhou, J.-S., Goodenough, J.B., (1996) Phys. Rev. B, 53, p. 14445Zhou, J.-S., Archibald, W., Goodenough, J.B., (1996) Nature (London), 381, p. 770Rao, G.H., Sun, J.R., Liang, J.K., Zhou, W.Y., Cheng, X.R., (1996) Appl. Phys. Lett., 69, p. 424Rao, G.H., Sun, J.R., Liang, J.K., Zhou, W.Y., (1997) Phys. Rev. B, 55, p. 3742Zhou, J.-S., Goodenough, J.B., (1998) Phys. Rev. Lett., 80, p. 2665Ibarra, M.R., Zhao, G.-M., De Teresa, J.M., García-Landa, B., Arnold, Z., Marquina, C., Algarabel, P.A., Ritter, C., (1998) Phys. Rev. B, 57, p. 7446Baszynski, J., Kovac, J., Kowalczyk, A., (1999) J. Magn. Magn. Mater., 195, p. 93Moritomo, Y., (1999) Phys. Rev. B, 60, p. 10374Young, R.A., Sakthivel, A., Moss, T.S., Paiva-Santos, C.O., (1995) J. Appl. Crystallogr., 28, p. 366Radaelli, P.G., Cox, D.E., Marezio, M., Cheong, S.-W., (1997) Phys. Rev. B, 55, p. 3015Huang, Q., Santoro, A., Lynn, J.W., Erwin, R.W., Borches, J.A., Peng, J.L., Ghosh, K., Greene, R.L., (1998) Phys. Rev. B, 58, p. 2684Irwin, J.C., Chrzanowski, J., Franck, J.P., (1999) Phys. Rev. B, 59, p. 9362Abrashev, M.V., Ivanov, V.G., Iliev, M.N., Chakalov, R.A., Chakalova, R.I., Thomsen, C., (1999) Phys. Status Solidi B, 215, p. 631Liarokapis, E., Leventouri, Th., Lampakis, D., Palles, D., Neumeier, J.J., Goodwin, D.H., (1999) Phys. Rev. B, 60, p. 12758Granado, E., Moreno, N.O., García, A., Sanjurjo, J.A., Rettori, C., Torriani, I., Oseroff, S.B., Tokura, Y., (1998) Phys. Rev. B, 58, p. 11435Yoon, S., Liu, H.L., Schollerer, G., Cooper, S.L., Han, P.D., Payne, D.A., Cheong, S.-W., Fisk, Z., (1998) Phys. Rev. B, 58, p. 2795Liu, H.L., Yoon, S., Cooper, S.L., Cheong, S.-W., Han, P.D., Payne, D.A., (1998) Phys. Rev. B, 58, pp. R10115Liu, K., Wu, X.W., Ahn, K.H., Sulchek, T., Chien, C.L., Xiao, J.Q., (1996) Phys. Rev. B, 54, p. 3007Granado, E., Pagliuso, P.G., Sanjurjo, J.A., Rettori, C., Oseroff, S.B., Causa, M.T., Butera, A., Schultz, S., (1998) Non-Crystalline and Nanoscale Materials, pp. 105-115. , edited by J. Rivas and M.A. López-Quintela (World Scientific, Singapore)Granado, E., Sanjurjo, J.A., Rettori, C., Prado, F., Sánchez, R.D., Caneiro, A., Oseroff, S.B., (2000) Phys. Status Solidi B, 220, p. 609Dediu, V., Ferdeghini, C., Matacotta, F.C., Nozar, P., Ruani, G., (2000) Phys. Rev. Lett., 84, p. 4489Adams, C.P., Lynn, J.W., Mukovskii, Y.M., Arsenov, A.A., Shulyatev, D.A., (2000) Phys. Rev. Lett., 85, p. 3954Dai, P., Fernandez-Baca, J.A., Wakabayashi, N., Plummer, E.W., Tomioka, Y., Tokura, Y., (2000) Phys. Rev. Lett., 85, p. 255

    Design of ideal vibrational signals for stinkbug male attraction through vibrotaxis experiments

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    Many groups of insects utilize substrate-borne vibrations for intraspecific communication. This characteristic makes them a suitable model for exploring the vibrations as a tool for pest control in alternative to chemicals. The detailed knowledge of the species communication is a prerequisite to select the best signals to use. In this sense, this study aimed at exploring the use of substrate-borne vibrations for pest control of the brown marmorated stink bug (BMSB), Halyomorpha halys Stål (Heteroptera: Pentatomidae). To this purpose, in a first set of experiments, we identified the spectral and temporal characteristics that best elicit male responsiveness. Bioassays were conducted with artificial signals that mimicked the natural female calling signal. In a second part, we used the acquired knowledge to synthesize new signals endowed with different degrees of attractiveness in single and two choice bioassays using a wooden custom-made T stand

    The genome of Bifidobacterium pseudocatenulatum IPLA 36007, a human intestinal strain with isoflavone-activation activity

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    Background: Bifidobacterium species, including Bifidobacterium pseudocatenulatum, are among the dominant microbial populations of the human gastrointestinal tract. They are also major components of many commercial probiotic products. Resident and transient bifidobacteria are thought to have several beneficial health effects. However, our knowledge of how these bacteria interact and communicate with host cells remains poor. This knowledge is essential for scientific support of their purported health benefits and their rational inclusion in functional foods. Results: This work describes the draft genome sequence of Bifidobacterium pseudocatenulatum IPLA 36007, a strain isolated as dominant from the feces of a healthy human. Besides several properties of probiosis, IPLA 36007 exhibited the capability of releasing aglycones from soy isoflavone glycosides. The genome contains 1,851 predicted genes, including 54 genes for tRNAs and fie copies of unique 16S, 23S and 5S rRNA genes. As key attributes of the IPLA 36007 genome we can mention the presence of a lysogenic phage, a cluster encoding type IV fimbriae, and a locus encoding a clustered, regularly interspaced, short, palindromic repeat (CRISPR)-Cas system. Four open reading frames (orfs) encoding \u3b2-glucosidases belonging to the glycosyl hydrolase family 3, which may act on isoflavone glycosides, were encountered. Additionally, one gene was found to code for a glycosyl hydrolase of family 1 that might also have \u3b2-glucosidase activity. Conclusion: The availability of the B. pseudocatenulatum IPLA 36007 genome should allow the enzyme system involved in the release of soy isoflavone aglycones from isoflavone glycosides, and the molecular mechanisms underlying the strain's probiotic properties, to be more easily understood

    Altered miRNA processing disrupts brown/white adipocyte determination and associates with lipodystrophy

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    miRNAs are important regulators of biological processes in many tissues, including the differentiation and function of brown and white adipocytes. the endoribonuclease dicer is a major component of the miRNA-processing pathway, and in adipose tissue, levels of dicer have been shown to decrease with age, increase with caloric restriction, and influence stress resistance. Here, we demonstrated that mice with a fat-specific KO of dicer develop a form of lipodystrophy that is characterized by loss of intra-abdominal and subcutaneous white fat, severe insulin resistance, and enlargement and whitening of interscapular brown fat. Additionally, KO of dicer in cultured brown preadipocytes promoted a white adipocyte-like phenotype and reduced expression of several miRNAs. Brown preadipocyte whitening was partially reversed by expression of miR-365, a miRNA known to promote brown fat differentiation; however, introduction of other miRNAs, including miR-346 and miR-362, also contributed to reversal of the loss of the dicer phenotype. Interestingly, fat samples from patients with HIV-related lipodystrophy exhibited a substantial downregulation of dicer mRNA expression. Together, these findings indicate the importance of miRNA processing in white and brown adipose tissue determination and provide a potential link between this process and HIV-related lipodystrophy.NIHEllison FoundationJoslin Diabetes and Endocrinology Research Center coresMary K. Iacocca ProfessorshipAcademy of FinlandSigrid Juselius FoundationFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Harvard Univ, Sch Med, Joslin Diabet Ctr, Sect Integrat Physiol & Metab, Boston, MA 02115 USAUniversidade Federal de São Paulo, Dept Biophys, São Paulo, BrazilUniversidade Federal de São Paulo, Program Mol Biol, São Paulo, BrazilAstraZeneca R&D, Cardiovasc & Metab Dis iMed, Molndal, SwedenUniv Helsinki, Dept Med, Helsinki, FinlandMinerva Fdn, Inst Med Res, Helsinki, FinlandUniv Massachusetts, Sch Med, Program Mol Med, Worcester, MA USAMassachusetts Gen Hosp, Program Nutr Metab, Boston, MA 02114 USAHarvard Univ, Sch Med, Boston, MA USAUniversidade Federal de São Paulo, Dept Biophys, São Paulo, BrazilUniversidade Federal de São Paulo, Program Mol Biol, São Paulo, BrazilNIH: DK082659NIH: DK033201NIH: AI060354NIH: DK040561NIH: U24-DK093000Joslin Diabetes and Endocrinology Research Center cores: DK036836FAPESP: 2010/52557-0Web of Scienc
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