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Research Article

Presence of a pertussis toxin-sensitive G protein α subunit in Sporothrix schenckii

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Pages 109-121 | Published online: 09 Jul 2009

References

  • Travassos LR, Lloyd KO. Sporothrix schenckii and related species of Ceratocystis. Microbiol Rev 1980; 44: 683–721.
  • Betancourt S, Torres-Bauza LJ, Rodriguez-del Valle N. Molec-ular and cellular events during the yeast to mycelium transition in Sporothrix schenckii. Sabouraudia: J Med Vet Mycol 1985; 23: 207–218.
  • Resto S, Rodriguez-del Valle N. Yeast cell cycle of Sporothrix schenckii. J Med Vet Mycol 1988; 26: 13–24.
  • Rodriguez-del Valle N, Rosario M, Torres-Blasini G. Effects of pH, temperature, aeration, and carbon source on the develop-ment of the mycelial and yeast forms of Sporothrix schenckii. Mycopathologia 1983; 8/ 83–88.
  • Alsina A, Rodriguez-del Valle N. Effects of divalent cations and functionally related substances on the yeast to mycelium transition in Sporothrix schenckii. Sabouraudia: J Med Vet Mycol 1984; 22: 1–5.
  • Rivera-Rodriguez N, Rodriguez-del Valle N. Effects of calcium ions on the germination of Sporothrix schenckii conidia. J Med Vet Mycol 1992; 30: 185–195.
  • Serrano S, Rodriguez-del Valle N. Calcium uptake and efflux during the yeast to mycelium transition in Sporothrix schenckii. Mycopathologia 1990; 112: 1–9.
  • Rodriguez-del Valle N, Rodriguez-Medina JR. Calcium stimu-lates molecular and cellular events during the yeast-to-mycelium transition in Sporothrix schenckii. J Med Vet Mycol 1993; 31: 43–53.
  • Rodriguez-del Valle N, Debs-Elias N, Alsina A. Effects of caffeine, cyclic 3', 5' adenosine monophosphate and cyclic 3', 5' guanosine monophosphate in the development of the mycelial form of Sporothrix schenckii. Mycopathologia 1984; 86: 29–33.
  • Co16n-Colón W, Rodriguez-del Valle N. Studies on phase transitions in Sporothrix schenckii: Possible involvement of Protein Kinase C. In: Vanden Bossche H, Odds FC, Kerridge D, eds. Dimorphic Fungi in Biology and Medicine. New York: Plenum Publishing Co, 1993: 225–239.
  • Hamm HE, Gilchrist A. Heterotrimeric G proteins. Curr Opin Cell Biol 1996; 8: 189–196.
  • Kaziro Y, Itoh H, Kozasa T, Nakafuku M, Satoh T. Structure and function of signal-transducing GTP-binding proteins. Ann Rev Biochem 1991; 60: 349–400.
  • Sprang SR. G protein mechanisms: Insights from structural analysis. Annu Rev Biochem 1997; 66: 639–678.
  • Rens-Dimiano S, Hamm HE. Structural and functional rela-tionships of heterotrimeric G-proteins. FASEB J 1995; 9: 1059–1066.
  • Wilkie TM, Yokoyama S. Evolution of the G protein alpha subunit multigene family. In: Molecular Evolution of Physiolog-ical Processes. New York: Rockefeller University Press, 1994: 249–270.
  • Baldwin JM. Structure and function of receptors coupled to G proteins. Curr Opin Cell Biol 1994; 6: 180–190.
  • Furukawa T, Miura R, Mori Y, et al. Differential interactions of the C terminus and the cytoplasmicI-II loop of neuronal Ca' ± channels with G-protein a and 137 subunits. J Biol Chem 1998; 273: 17595–17603.
  • Herlitze S, Garcia DE, Mackie K, Hillie B, Scheuer T, Catterall WA. Modulation of Ca2 ± channels by G-protein 137 subunits. Nature 1996; 380: 258–262.
  • Taussig R,JA, Gilman AG. Inhibition of adeny-ly1 cyclase by G,.. Science 1993; 261: 218–221.
  • Simon MI, Strathmann MP, Gautam N. Diversity of G proteins in signal transduction. Science 1991; 252: 802–808.
  • Buss JE, Mumby SM, Casey PJ, Gilman AG, Sefton BM. Myristoylated a subunits of guanine nucleotide-binding regula-tory proteins. Proc Natl Acad Sci USA 1987; 84: 7493–7497.
  • Scheuring J, Berri PJ, Schramm VL. Transition-state structure for the ADP-ribosylation of recombinant G.,1 subunits by pertussis toxin. Biochemistry 1998; 37: 2748–2758.
  • West RE, Moss J, Vaughan M, Liu T, Liu TY. Pertussis toxin-catalyzed ADP-ribosylation of transducin. J Biol Chem 1985; 260: 14428–14430.
  • Stryer L. Cyclic GMP cascade of vision. Ann Rev Neurosci 1986; 9: 87–119.
  • Stoyanov B, Volinia S, Hanck T, et al. Cloning and characteri-zation of a G protein-activated human phosphoinositide-3 ki-nase. Science 1995; 269: 690–693.
  • Brown AM. Ionic channels and their regulation by G protein subunits. Ann Rev Physiol 1990; 52: 197–213.
  • Kusakabe Y, Yamaguchi E, Tanemura K, et al. Identification of two a-subunit species of GTP-binding proteins, Gc,15 and G„,,, expressed in rat taste buds. Biochim Biophys Acta 1998; 1403: 265–272.
  • Exton JH. Cell signaling through guanine-nucleotide-binding regulatory proteins (G proteins) and phospholipases. Eur J Biochem 1997; 243: 10–20.
  • Voyno-Yasenetskaya TA, Conklin BR, Gilbert RL, Hooley R, Bourne HR, Barber DL. Gc,13 stimulates Na-H exchange. J Biol Chem 1994; 269: 4721–4724.
  • Nakafuku M, Itoh H, Nakamura S, Kaziro Y. Occurrence in Saccharomyces cerevisiae of a gene homologous to the cDNA coding for the a subunits of mammalian G proteins. Proc Natl Acad Sci USA 1987; 84: 2140–2144.
  • Nakafuku M, Obara T, Kaibuchi K, et al. Isolation of a second yeast Saccharomyces cerevisiae gene (GPA2) coding for guanine nucleotide-binding regulatory protein: studies on its structure and possible functions. Proc Natl Acad Sci USA 1988; 85: 1374–1378.
  • Sadhu C, Hekstra D, McEachern MJ, Reed SI, Hicks JB. A G protein a subunit from asexual Candida albicans functions in the mating signal-transduction pathway of Saccharomyces cere-visiae and is regulated by the aI-a2 repressor. Mol Cell Biol 1992; 12: 1977–1985.
  • Saviiión-Tejada AL, Ongay-Larios L, Ramirez J, Coria R. Isolation of a gene encoding a G protein a subunit involved in the regulation of cAMP levels in the yeast Kluyveromyces lactis. Yeast 1996; 12: 1125–1133.
  • Tolkacheva T, McNamara P, Piekarz E, Courchesne W. Cloning of a Cryptococcus neoformans gene, GPA1, encoding a G-protein a-subunit homolog. Infec Immun 1994; 62: 2849–2856.
  • Ma H, Yanofski MF, Meyerowitz EM. Molecular cloning and characterization of GPA1, a G protein a subunit gene from Arabidopsis thaliana. Proc Natl Acad Sci USA 1990; 87: 3821–3825.
  • Smulian AG, Ryan M, Staben C, Cushion MT. Signal trans-duction in Pneurnocystis carinii: characterization of the genes (pcgl) encoding the alpha subunit of the G protein (PCG1) of Pneumocystis carinii carinii and Pneumocystis carinii ratti. Infect Immun 1996; 64: 691–701.
  • Alspaugh JA, Perfect JR, Heitman J. Cryptococcus neoformans mating and virulence are regulated by the G-protein a subunit GPA1 and cAMP. Genes Dev 1997; 11: 3206–3217.
  • Turner GE, Borkovich KA. Identification of a G protein a subunit from Neurospora crassa that is a member of the G, family. J Biol Chem 1993; 268: 14805–14811.
  • Ivey FD, Hodge PN, Turner GE, Borkovich KA. The Gc„ Homologue gna-1 controls multiple differentiation pathways in Neurospora crassa. Mol Biol Cell 1996; 7: 1283–1297.
  • Yu JH, Wieser J, Adams TH. The Aspergillus FlbA RGS domain protein antagonizes G protein signaling to block prolif-eration and allow development. EMBO J 1996; 15: 5184–5190.
  • Choi GH, Chen B, Nuss D. Virus-mediated or transgenic suppression of a G-protein a subunit and attenuation of fungal virulence. Proc Natl Acad Sci USA 1995; 92: 305–309.
  • Regenfelder E, Spellig T, Hartmann A, Lauenstein S, Bolker M, Kahmann R. G proteins in Ustilago maydis: transmission of multiple signals? EMBO J 1997; 16: 1934-1942.
  • Liu S, Dean RA. G protein a subunit genes control growth, development, and pathogenicity of Magnaporthe grisea. Mol Plant-Microb Interact 1997; 10: 1075–1086.
  • Mendonça L, Gorin PAJ, Lloyd KO, Travassos LR. Polymor-phism of Sporothrix schenckii surface polysaccharides as a function of morphological differentiation. Biochemistry 1976; 15: 2423–2425.
  • Aquino-Pifiero EF, Rodríguw-del Valle N. Different protein kinase C isofonns are present in the yeast and mycelium forms of Sporothrix schenckii. Mycopathologia 1997; 138: 109–115.
  • Bowman El, Bowman BJ. Purification of vacuolar membranes, mitochondria, and plasma membranes from Neurospora crassa and modes of discriminating among different H -F-ATPases. Methods Enzymol 1988; 157: 562–571.
  • Laemmli UK. Cleavage of structural proteins during assembly of the bacteriophage T4. Nature 1970; 227: 680–685.
  • Carty DJ. Pertussis toxin-catalyzed ADP-ribosylation of G proteins. Methods Enzymol 1994; 237: 63–70.
  • Sherman F, Fink GR, Hicks JB. Methods in Yeast Genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 1986.
  • Chomczynski P, Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 1987; 162: 156–159.
  • Wilkie TM, Aragay AM, Watson AJ, Simon MI. Design of degenerate oligonucleotide primers for cloning of G-protein subunits. Methods Enzymo11994; 237: 327–344.
  • Sambrook J, Fritsch EF, Maniatis T. Molecular Cloning: A Laboratory Manual. 2nd edn. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 1989.
  • Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ. Basic local alignment search tool. J Mol Biol 1990; 215: 403–410.
  • Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improv-ing the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994; 22: 4673–4680.
  • Martinez-Cadena G, Novoa-Martinez G, Gonzalez-Hernandez A, Garcia-Soto J. The GTP-binding protein G alpha s is present in dormant spores and expressed differentially during spore germination of the fungus Phycomyces blakesleeanus. Microbiol-ogy 1995; 141: 3149–3154.
  • Raport CJ, Dere B, Hurley JB. Characterization of the mouse rod transducin a subunit gene. J Biol Chem 1989; 264: 7122–7128.

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