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Volumn 7, Issue 7, 2012, Pages

Pharyngeal polysaccharide deacetylases affect development in the nematode C. elegans and deacetylate chitin in vitro

Author keywords

[No Author keywords available]

Indexed keywords

CHITIN; CHITOSAN; EOSIN; POLYSACCHARIDE; POLYSACCHARIDE DEACETYLASE; UNCLASSIFIED DRUG;

EID: 84863768150     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0040426     Document Type: Article
Times cited : (24)

References (30)
  • 1
    • 33646917247 scopus 로고    scopus 로고
    • The cyst wall of Entamoeba invadens contains chitosan (deacetylated chitin)
    • Das S, Van Dellen K, Bulik D, Magnelli P, Cui J, et al. (2006) The cyst wall of Entamoeba invadens contains chitosan (deacetylated chitin). Mol Biochem Parasitol 148: 86-92.
    • (2006) Mol Biochem Parasitol , vol.148 , pp. 86-92
    • Das, S.1    van Dellen, K.2    Bulik, D.3    Magnelli, P.4    Cui, J.5
  • 2
    • 27744569817 scopus 로고    scopus 로고
    • A chitin synthase and its regulator protein are critical for chitosan production and growth of the fungal pathogen Cryptococcus neoformans
    • Banks IR, Specht CA, Donlin MJ, Gerik KJ, Levitz SM, et al. (2005) A chitin synthase and its regulator protein are critical for chitosan production and growth of the fungal pathogen Cryptococcus neoformans. Eukaryot Cell 4: 1902-1912.
    • (2005) Eukaryot Cell , vol.4 , pp. 1902-1912
    • Banks, I.R.1    Specht, C.A.2    Donlin, M.J.3    Gerik, K.J.4    Levitz, S.M.5
  • 3
    • 34249736906 scopus 로고    scopus 로고
    • Chitosan, the deacetylated form of chitin, is necessary for cell wall integrity in Cryptococcus neoformans
    • Baker LG, Specht CA, Donlin MJ, Lodge JK, (2007) Chitosan, the deacetylated form of chitin, is necessary for cell wall integrity in Cryptococcus neoformans. Eukaryot Cell 6: 855-867.
    • (2007) Eukaryot Cell , vol.6 , pp. 855-867
    • Baker, L.G.1    Specht, C.A.2    Donlin, M.J.3    Lodge, J.K.4
  • 4
    • 67349149610 scopus 로고    scopus 로고
    • Analysis of functions of the chitin deacetylase gene family in Tribolium castaneum
    • Arakane Y, Dixit R, Begum K, Park Y, Specht CA, et al. (2009) Analysis of functions of the chitin deacetylase gene family in Tribolium castaneum. Insect Biochem Mol Biol 39: 355-365.
    • (2009) Insect Biochem Mol Biol , vol.39 , pp. 355-365
    • Arakane, Y.1    Dixit, R.2    Begum, K.3    Park, Y.4    Specht, C.A.5
  • 5
    • 30944456679 scopus 로고    scopus 로고
    • serpentine and vermiform encode matrix proteins with chitin binding and deacetylation domains that limit tracheal tube length in Drosophila
    • Luschnig S, Batz T, Armbruster K, Krasnow MA, (2006) serpentine and vermiform encode matrix proteins with chitin binding and deacetylation domains that limit tracheal tube length in Drosophila. Curr Biol 16: 186-194.
    • (2006) Curr Biol , vol.16 , pp. 186-194
    • Luschnig, S.1    Batz, T.2    Armbruster, K.3    Krasnow, M.A.4
  • 6
    • 30944448000 scopus 로고    scopus 로고
    • Septate-junction-dependent luminal deposition of chitin deacetylases restricts tube elongation in the Drosophila trachea
    • Wang S, Jayaram SA, Hemphala J, Senti KA, Tsarouhas V, et al. (2006) Septate-junction-dependent luminal deposition of chitin deacetylases restricts tube elongation in the Drosophila trachea. Curr Biol 16: 180-185.
    • (2006) Curr Biol , vol.16 , pp. 180-185
    • Wang, S.1    Jayaram, S.A.2    Hemphala, J.3    Senti, K.A.4    Tsarouhas, V.5
  • 7
    • 40649107148 scopus 로고    scopus 로고
    • Domain organization and phylogenetic analysis of proteins from the chitin deacetylase gene family of Tribolium castaneum and three other species of insects
    • Dixit R, Arakane Y, Specht CA, Richard C, Kramer KJ, et al. (2008) Domain organization and phylogenetic analysis of proteins from the chitin deacetylase gene family of Tribolium castaneum and three other species of insects. Insect Biochem Mol Biol 38: 440-451.
    • (2008) Insect Biochem Mol Biol , vol.38 , pp. 440-451
    • Dixit, R.1    Arakane, Y.2    Specht, C.A.3    Richard, C.4    Kramer, K.J.5
  • 8
    • 0027531525 scopus 로고
    • Rhizobium NodB protein involved in nodulation signal synthesis is a chitooligosaccharide deacetylase
    • John M, Rohrig H, Schmidt J, Wieneke U, Schell J, (1993) Rhizobium NodB protein involved in nodulation signal synthesis is a chitooligosaccharide deacetylase. Proc Natl Acad Sci U S A 90: 625-629.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 625-629
    • John, M.1    Rohrig, H.2    Schmidt, J.3    Wieneke, U.4    Schell, J.5
  • 9
    • 0036468361 scopus 로고    scopus 로고
    • Regulation of organogenesis by the Caenorhabditis elegans FoxA protein PHA-4
    • Gaudet J, Mango SE, (2002) Regulation of organogenesis by the Caenorhabditis elegans FoxA protein PHA-4. Science 295: 821-825.
    • (2002) Science , vol.295 , pp. 821-825
    • Gaudet, J.1    Mango, S.E.2
  • 10
    • 26244457216 scopus 로고    scopus 로고
    • A novel chitin-binding protein identified from the peritrophic membrane of the cabbage looper, Trichoplusia ni
    • Guo W, Li G, Pang Y, Wang P, (2005) A novel chitin-binding protein identified from the peritrophic membrane of the cabbage looper, Trichoplusia ni. Insect Biochem Mol Biol 35: 1224-1234.
    • (2005) Insect Biochem Mol Biol , vol.35 , pp. 1224-1234
    • Guo, W.1    Li, G.2    Pang, Y.3    Wang, P.4
  • 11
    • 0032476041 scopus 로고    scopus 로고
    • Heparan sulfate/heparin N-deacetylase/N-sulfotransferase. The N-sulfotransferase activity domain is at the carboxyl half of the holoenzyme
    • Berninsone P, Hirschberg CB, (1998) Heparan sulfate/heparin N-deacetylase/N-sulfotransferase. The N-sulfotransferase activity domain is at the carboxyl half of the holoenzyme. J Biol Chem 273: 25556-25559.
    • (1998) J Biol Chem , vol.273 , pp. 25556-25559
    • Berninsone, P.1    Hirschberg, C.B.2
  • 12
  • 13
    • 3142568420 scopus 로고    scopus 로고
    • Structures of Bacillus subtilis PdaA, a family 4 carbohydrate esterase, and a complex with N-acetyl-glucosamine
    • Blair DE, van Aalten DM, (2004) Structures of Bacillus subtilis PdaA, a family 4 carbohydrate esterase, and a complex with N-acetyl-glucosamine. FEBS Lett 570: 13-19.
    • (2004) FEBS Lett , vol.570 , pp. 13-19
    • Blair, D.E.1    van Aalten, D.M.2
  • 14
    • 27344441825 scopus 로고    scopus 로고
    • Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor
    • Blair DE, Schuttelkopf AW, MacRae JI, van Aalten DM, (2005) Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor. Proc Natl Acad Sci U S A 102: 15429-15434.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 15429-15434
    • Blair, D.E.1    Schuttelkopf, A.W.2    MacRae, J.I.3    van Aalten, D.M.4
  • 15
    • 33747106199 scopus 로고    scopus 로고
    • Structure and mechanism of chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum
    • Blair DE, Hekmat O, Schuttelkopf AW, Shrestha B, Tokuyasu K, et al. (2006) Structure and mechanism of chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum. Biochemistry 45: 9416-9426.
    • (2006) Biochemistry , vol.45 , pp. 9416-9426
    • Blair, D.E.1    Hekmat, O.2    Schuttelkopf, A.W.3    Shrestha, B.4    Tokuyasu, K.5
  • 16
    • 0037373288 scopus 로고    scopus 로고
    • Caenorhabditis elegans exoskeleton collagen COL-19: an adult-specific marker for collagen modification and assembly, and the analysis of organismal morphology
    • Thein MC, McCormack G, Winter AD, Johnstone IL, Shoemaker CB, et al. (2003) Caenorhabditis elegans exoskeleton collagen COL-19: an adult-specific marker for collagen modification and assembly, and the analysis of organismal morphology. Dev Dyn 226: 523-539.
    • (2003) Dev Dyn , vol.226 , pp. 523-539
    • Thein, M.C.1    McCormack, G.2    Winter, A.D.3    Johnstone, I.L.4    Shoemaker, C.B.5
  • 17
    • 0034884938 scopus 로고    scopus 로고
    • Nematode chitin synthases: gene structure, expression and function in Caenorhabditis elegans and the plant parasitic nematode Meloidogyne artiellia
    • Veronico P, Gray LJ, Jones JT, Bazzicalupo P, Arbucci S, et al. (2001) Nematode chitin synthases: gene structure, expression and function in Caenorhabditis elegans and the plant parasitic nematode Meloidogyne artiellia. Mol Genet Genomics 266: 28-34.
    • (2001) Mol Genet Genomics , vol.266 , pp. 28-34
    • Veronico, P.1    Gray, L.J.2    Jones, J.T.3    Bazzicalupo, P.4    Arbucci, S.5
  • 18
    • 17044387281 scopus 로고    scopus 로고
    • Analysis of chitin synthase function in a plant parasitic nematode, Meloidogyne artiellia, using RNAi
    • Fanelli E, Di Vito M, Jones JT, De Giorgi C, (2005) Analysis of chitin synthase function in a plant parasitic nematode, Meloidogyne artiellia, using RNAi. Gene 349: 87-95.
    • (2005) Gene , vol.349 , pp. 87-95
    • Fanelli, E.1    Di Vito, M.2    Jones, J.T.3    de Giorgi, C.4
  • 19
    • 25844460448 scopus 로고    scopus 로고
    • The chitin synthase genes chs-1 and chs-2 are essential for C. elegans development and responsible for chitin deposition in the eggshell and pharynx, respectively
    • Zhang Y, Foster JM, Nelson LS, Ma D, Carlow CK, (2005) The chitin synthase genes chs-1 and chs-2 are essential for C. elegans development and responsible for chitin deposition in the eggshell and pharynx, respectively. Dev Biol 285: 330-339.
    • (2005) Dev Biol , vol.285 , pp. 330-339
    • Zhang, Y.1    Foster, J.M.2    Nelson, L.S.3    Ma, D.4    Carlow, C.K.5
  • 20
    • 0037031152 scopus 로고    scopus 로고
    • Loss of the putative RNA-directed RNA polymerase RRF-3 makes C. elegans hypersensitive to RNAi
    • Simmer F, Tijsterman M, Parrish S, Koushika SP, Nonet ML, et al. (2002) Loss of the putative RNA-directed RNA polymerase RRF-3 makes C. elegans hypersensitive to RNAi. Curr Biol 12: 1317-1319.
    • (2002) Curr Biol , vol.12 , pp. 1317-1319
    • Simmer, F.1    Tijsterman, M.2    Parrish, S.3    Koushika, S.P.4    Nonet, M.L.5
  • 21
    • 0037470792 scopus 로고    scopus 로고
    • Carbohydrate esterase family 4 enzymes: substrate specificity
    • Caufrier F, Martinou A, Dupont C, Bouriotis V, (2003) Carbohydrate esterase family 4 enzymes: substrate specificity. Carbohydr Res 338: 687-692.
    • (2003) Carbohydr Res , vol.338 , pp. 687-692
    • Caufrier, F.1    Martinou, A.2    Dupont, C.3    Bouriotis, V.4
  • 22
    • 79959360452 scopus 로고    scopus 로고
    • Stage-specific proteomic expression patterns of the human filarial parasite Brugia malayi and its endosymbiont Wolbachia
    • Bennuru S, Meng Z, Ribeiro JM, Semnani RT, Ghedin E, et al. (2011) Stage-specific proteomic expression patterns of the human filarial parasite Brugia malayi and its endosymbiont Wolbachia. Proc Natl Acad Sci U S A 108: 9649-9654.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 9649-9654
    • Bennuru, S.1    Meng, Z.2    Ribeiro, J.M.3    Semnani, R.T.4    Ghedin, E.5
  • 23
    • 33746931270 scopus 로고    scopus 로고
    • C. elegans pharyngeal morphogenesis requires both de novo synthesis of pyrimidines and synthesis of heparan sulfate proteoglycans
    • Franks DM, Izumikawa T, Kitagawa H, Sugahara K, Okkema PG, (2006) C. elegans pharyngeal morphogenesis requires both de novo synthesis of pyrimidines and synthesis of heparan sulfate proteoglycans. Dev Biol 296: 409-420.
    • (2006) Dev Biol , vol.296 , pp. 409-420
    • Franks, D.M.1    Izumikawa, T.2    Kitagawa, H.3    Sugahara, K.4    Okkema, P.G.5
  • 24
    • 0037406616 scopus 로고    scopus 로고
    • A profile of putative parasitism genes expressed in the esophageal gland cells of the root-knot nematode Meloidogyne incognita
    • Huang G, Gao B, Maier T, Allen R, Davis EL, et al. (2003) A profile of putative parasitism genes expressed in the esophageal gland cells of the root-knot nematode Meloidogyne incognita. Mol Plant Microbe Interact 16: 376-381.
    • (2003) Mol Plant Microbe Interact , vol.16 , pp. 376-381
    • Huang, G.1    Gao, B.2    Maier, T.3    Allen, R.4    Davis, E.L.5
  • 25
    • 0029898363 scopus 로고    scopus 로고
    • Temporal reiteration of a precise gene expression pattern during nematode development
    • Johnstone IL, Barry JD, (1996) Temporal reiteration of a precise gene expression pattern during nematode development. EMBO J 15: 3633-3639.
    • (1996) EMBO J , vol.15 , pp. 3633-3639
    • Johnstone, I.L.1    Barry, J.D.2
  • 27
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment
    • Kumar S, Tamura K, Nei M, (2004) MEGA3: Integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment. Brief Bioinform 5: 150-163.
    • (2004) Brief Bioinform , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 28
    • 0038725897 scopus 로고    scopus 로고
    • Genome-wide RNAi screening in Caenorhabditis elegans
    • Kamath RS, Ahringer J, (2003) Genome-wide RNAi screening in Caenorhabditis elegans. Methods 30: 313-321.
    • (2003) Methods , vol.30 , pp. 313-321
    • Kamath, R.S.1    Ahringer, J.2
  • 29
    • 0025102841 scopus 로고
    • Detection of chitin deacetylase activity after polyacrylamide gel electrophoresis
    • Trudel J, Asselin A, (1990) Detection of chitin deacetylase activity after polyacrylamide gel electrophoresis. Anal Biochem 189: 249-253.
    • (1990) Anal Biochem , vol.189 , pp. 249-253
    • Trudel, J.1    Asselin, A.2
  • 30
    • 0142184966 scopus 로고    scopus 로고
    • Chitin synthesis in Saccharomyces cerevisiae in response to supplementation of growth medium with glucosamine and cell wall stress
    • Bulik DA, Olczak M, Lucero HA, Osmond BC, Robbins PW, et al. (2003) Chitin synthesis in Saccharomyces cerevisiae in response to supplementation of growth medium with glucosamine and cell wall stress. Eukaryot Cell 2: 886-900.
    • (2003) Eukaryot Cell , vol.2 , pp. 886-900
    • Bulik, D.A.1    Olczak, M.2    Lucero, H.A.3    Osmond, B.C.4    Robbins, P.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.