메뉴 건너뛰기




Volumn 5, Issue , 2015, Pages

Yeast nitrogen utilization in the phyllosphere during plant lifespan under regulation of autophagy

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS PROTEIN; AUTOPHAGY-RELATED11 PROTEIN, ARABIDOPSIS; METHYLAMINE; NITRATE REDUCTASE; NITROGEN; VESICULAR TRANSPORT PROTEIN;

EID: 84928401808     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep09719     Document Type: Article
Times cited : (15)

References (50)
  • 1
    • 0141959524 scopus 로고    scopus 로고
    • Fifty years of phyllosphere microbiology: Significant contributions to research in related fields
    • Lindow, S., Hecht-Poinar, E. & Elliott, V. (ed.) St. Paul, MN, USA: APS Press
    • Morris, C. & Kinkel, L. Fifty years of phyllosphere microbiology: significant contributions to research in related fields. In Lindow, S., Hecht-Poinar, E. & Elliott, V. (ed.), Phyllosphere microbiology, St. Paul, MN, USA: APS Press, 365-375 (2002).
    • (2002) Phyllosphere Microbiology , pp. 365-375
    • Morris, C.1    Kinkel, L.2
  • 2
  • 3
    • 56649114468 scopus 로고    scopus 로고
    • Phyllosphere microbiology with special reference to diversity and plant genotype
    • Whipps, J. M., Hand, P., Pink, D. & Bending, G. D. Phyllosphere microbiology with special reference to diversity and plant genotype. J. Appl. Microbiol. 105, 1744-55 (2008).
    • (2008) J. Appl. Microbiol. , vol.105 , pp. 1744-1755
    • Whipps, J.M.1    Hand, P.2    Pink, D.3    Bending, G.D.4
  • 5
    • 84882769607 scopus 로고    scopus 로고
    • Dominant colonization and inheritance of Methylobacterium sp. Strain OR01 on perilla plants
    • Mizuno, M., Yurimoto, H., Iguchi, H., Tani, A. & Sakai, Y. Dominant colonization and inheritance of Methylobacterium sp. strain OR01 on perilla plants. Biosci. Biotechnol. Biochem. 77, 1533-8 (2013).
    • (2013) Biosci. Biotechnol. Biochem. , vol.77 , pp. 1533-1538
    • Mizuno, M.1    Yurimoto, H.2    Iguchi, H.3    Tani, A.4    Sakai, Y.5
  • 7
    • 77952672792 scopus 로고    scopus 로고
    • Site and plant species are important determinants of the Methylobacterium community composition in the plant phyllosphere
    • Knief, C., Ramette, A., Frances, L., Alonso-Blanco, C. & Vorholt, J. A. Site and plant species are important determinants of the Methylobacterium community composition in the plant phyllosphere. ISME J. 4, 719-728 (2010).
    • (2010) ISME J. , vol.4 , pp. 719-728
    • Knief, C.1    Ramette, A.2    Frances, L.3    Alonso-Blanco, C.4    Vorholt, J.A.5
  • 8
    • 84856213023 scopus 로고    scopus 로고
    • Characterization of Methylobacterium strains isolated from the phyllosphere and description of Methylobacterium longum sp. Nov
    • Knief, C., Dengler, V., Bodelier, P. L. & Vorholt, J. A. Characterization of Methylobacterium strains isolated from the phyllosphere and description of Methylobacterium longum sp. nov. Antonie Van Leeuwenhoek 101, 169-83 (2012).
    • (2012) Antonie Van Leeuwenhoek , vol.101 , pp. 169-183
    • Knief, C.1    Dengler, V.2    Bodelier, P.L.3    Vorholt, J.A.4
  • 9
    • 79960201228 scopus 로고    scopus 로고
    • Detection and isolation of chloromethane-degrading bacteria from the Arabidopsis thaliana phyllosphere, and characterization of chloromethane utilization genes
    • Nadalig, T. et al. Detection and isolation of chloromethane-degrading bacteria from the Arabidopsis thaliana phyllosphere, and characterization of chloromethane utilization genes. FEMS Microbiol. Ecol. 77, 438-48 (2011).
    • (2011) FEMS Microbiol. Ecol. , vol.77 , pp. 438-448
    • Nadalig, T.1
  • 10
    • 84879835718 scopus 로고    scopus 로고
    • Methylobacterium trifolii sp. Nov and Methylobacterium thuringiense sp. Nov., Methanol-utilizing, pink-pigmented bacteria isolated from leaf surfaces
    • Wellner, S., Lodders, N., Glaeser, S. P. & Kampfer, P. Methylobacterium trifolii sp. nov. and Methylobacterium thuringiense sp. nov., methanol-utilizing, pink-pigmented bacteria isolated from leaf surfaces. Int. J. Syst. Evol. Microbiol. 63, 2690-9 (2013).
    • (2013) Int. J. Syst. Evol. Microbiol. , vol.63 , pp. 2690-2699
    • Wellner, S.1    Lodders, N.2    Glaeser, S.P.3    Kampfer, P.4
  • 12
    • 58149133837 scopus 로고    scopus 로고
    • Structure and function of denitrifying and nitrifying bacterial communities in relation to the plant species in a constructed wetland
    • Ruiz-Rueda, O., Hallin, S. & Baneras, L. Structure and function of denitrifying and nitrifying bacterial communities in relation to the plant species in a constructed wetland. FEMS Microbiol. Ecol. 67, 308-319 (2009).
    • (2009) FEMS Microbiol. Ecol. , vol.67 , pp. 308-319
    • Ruiz-Rueda, O.1    Hallin, S.2    Baneras, L.3
  • 13
    • 70349481520 scopus 로고    scopus 로고
    • Community proteogenomics reveals insights into the physiology of phyllosphere bacteria
    • Delmotte, N. et al. Community proteogenomics reveals insights into the physiology of phyllosphere bacteria. Proc. Natl. Acad. Sci. U. S. A. 106, 16428-33 (2009).
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 16428-16433
    • Delmotte, N.1
  • 14
    • 84871904349 scopus 로고    scopus 로고
    • Contribution of Nitrate Assimilation to the Fitness of Pseudomonas syringae pv. Syringae B728a on Plants
    • Parangan-Smith, A. & Lindow, S. Contribution of Nitrate Assimilation to the Fitness of Pseudomonas syringae pv. syringae B728a on Plants. Appl. Environ. Microbiol. 79, 678-687 (2013).
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 678-687
    • Parangan-Smith, A.1    Lindow, S.2
  • 15
    • 0001840999 scopus 로고
    • Nitrogen metabolism in Saccharomyces cerevisiae
    • Cooper, T. G. Nitrogen metabolism in Saccharomyces cerevisiae. Cold Spring Harbor Monograph Archive 11, 39-99 (1982).
    • (1982) Cold Spring Harbor Monograph Archive , vol.11 , pp. 39-99
    • Cooper, T.G.1
  • 16
    • 0027121435 scopus 로고
    • Hansenula polymorpha: An attractive model organism for molecular studies of peroxisome biogenesis and function
    • Veenhuis, M., van der Klei, I. J., Titorenko, V. & Harder, W. Hansenula polymorpha: an attractive model organism for molecular studies of peroxisome biogenesis and function. FEMS Microbiol. Lett. 100, 393-403 (1992).
    • (1992) FEMS Microbiol. Lett. , vol.100 , pp. 393-403
    • Veenhuis, M.1    Van Der Klei, I.J.2    Titorenko, V.3    Harder, W.4
  • 17
    • 0027420719 scopus 로고
    • Cloning and characterization of PAS5: A gene required for peroxisome biogenesis in the methylotrophic yeast Pichia pastoris
    • Spong, A. P. & Subramani, S. Cloning and characterization of PAS5: a gene required for peroxisome biogenesis in the methylotrophic yeast Pichia pastoris. J. Cell Biol. 123, 535-48 (1993).
    • (1993) J. Cell Biol. , vol.123 , pp. 535-548
    • Spong, A.P.1    Subramani, S.2
  • 18
    • 0032482219 scopus 로고    scopus 로고
    • Peroxisome degradation by microautophagy in Pichia pastoris: Identification of specific steps and morphological intermediates
    • Sakai, Y., Koller, A., Rangell, L. K., Keller, G. A. & Subramani, S. Peroxisome degradation by microautophagy in Pichia pastoris: identification of specific steps and morphological intermediates. J. Cell Biol. 141, 625-36 (1998).
    • (1998) J. Cell Biol. , vol.141 , pp. 625-636
    • Sakai, Y.1    Koller, A.2    Rangell, L.K.3    Keller, G.A.4    Subramani, S.5
  • 19
    • 66149184398 scopus 로고    scopus 로고
    • Atg26-mediated pexophagy is required for host invasion by the plant pathogenic fungus Colletotrichum orbiculare
    • Asakura, M. et al. Atg26-mediated pexophagy is required for host invasion by the plant pathogenic fungus Colletotrichum orbiculare. Plant Cell 21, 1291-304 (2009).
    • (2009) Plant Cell , vol.21 , pp. 1291-1304
    • Asakura, M.1
  • 20
    • 0036463736 scopus 로고    scopus 로고
    • Autophagy in the eukaryotic cell
    • Reggiori, F. & Klionsky, D. J. Autophagy in the eukaryotic cell. Eukaryot. Cell 1, 11-21 (2002).
    • (2002) Eukaryot. Cell , vol.1 , pp. 11-21
    • Reggiori, F.1    Klionsky, D.J.2
  • 22
    • 84871002139 scopus 로고    scopus 로고
    • Selective autophagy in budding yeast
    • Suzuki, K. Selective autophagy in budding yeast. Cell Death Differ. 20, 43-8 (2013).
    • (2013) Cell Death Differ. , vol.20 , pp. 43-48
    • Suzuki, K.1
  • 23
    • 57749121573 scopus 로고    scopus 로고
    • Mitophagy in yeast occurs through a selective mechanism
    • Kanki, T. & Klionsky, D. J. Mitophagy in yeast occurs through a selective mechanism. J. Biol. Chem. 283, 32386-93 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 32386-32393
    • Kanki, T.1    Klionsky, D.J.2
  • 24
    • 65949095803 scopus 로고    scopus 로고
    • Autophagy regulates lipid metabolism
    • Singh, R. et al. Autophagy regulates lipid metabolism. Nature 458, 1131-5 (2009).
    • (2009) Nature , vol.458 , pp. 1131-1135
    • Singh, R.1
  • 25
    • 43049138051 scopus 로고    scopus 로고
    • Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease
    • Kraft, C., Deplazes, A., Sohrmann, M. & Peter, M. Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease. Nat. Cell. Biol. 10, 602-10 (2008).
    • (2008) Nat. Cell. Biol. , vol.10 , pp. 602-610
    • Kraft, C.1    Deplazes, A.2    Sohrmann, M.3    Peter, M.4
  • 26
    • 34248581851 scopus 로고    scopus 로고
    • ER-phagy: Selective autophagy of the endoplasmic reticulum
    • Bernales, S., Schuck, S. & Walter, P. ER-phagy: selective autophagy of the endoplasmic reticulum. Autophagy 3, 285-7 (2007).
    • (2007) Autophagy , vol.3 , pp. 285-287
    • Bernales, S.1    Schuck, S.2    Walter, P.3
  • 27
    • 0035827541 scopus 로고    scopus 로고
    • Vacuolar localization of oligomeric alpha-mannosidase requires the cytoplasm to vacuole targeting and autophagy pathway components in Saccharomyces cerevisiae
    • Hutchins, M. U. & Klionsky, D. J. Vacuolar localization of oligomeric alpha-mannosidase requires the cytoplasm to vacuole targeting and autophagy pathway components in Saccharomyces cerevisiae. J. Biol. Chem. 276, 20491-8 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 20491-20498
    • Hutchins, M.U.1    Klionsky, D.J.2
  • 28
    • 79953850827 scopus 로고    scopus 로고
    • Aspartyl aminopeptidase is imported from the cytoplasm to the vacuole by selective autophagy in Saccharomyces cerevisiae
    • Yuga, M., Gomi, K., Klionsky, D. J. & Shintani, T. Aspartyl aminopeptidase is imported from the cytoplasm to the vacuole by selective autophagy in Saccharomyces cerevisiae. J. Biol. Chem. 286, 13704-13 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 13704-13713
    • Yuga, M.1    Gomi, K.2    Klionsky, D.J.3    Shintani, T.4
  • 29
    • 0029913505 scopus 로고    scopus 로고
    • Cytoplasm-to-vacuole targeting and autophagy employ the same machinery to deliver proteins to the yeast vacuole
    • Scott, S. V. et al. Cytoplasm-to-vacuole targeting and autophagy employ the same machinery to deliver proteins to the yeast vacuole. Proc. Natl. Acad. Sci. U. S. A. 93, 12304-8 (1996).
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 12304-12308
    • Scott, S.V.1
  • 30
    • 77950510302 scopus 로고    scopus 로고
    • The Cvt pathway as a model for selective autophagy
    • Lynch-Day, M. A. & Klionsky, D. J. The Cvt pathway as a model for selective autophagy. FEBS Lett. 584, 1359-66 (2010).
    • (2010) FEBS Lett. , vol.584 , pp. 1359-1366
    • Lynch-Day, M.A.1    Klionsky, D.J.2
  • 31
    • 59249105964 scopus 로고    scopus 로고
    • Monitoring autophagic degradation of p62/SQSTM1
    • Bjorkoy, G. et al. Monitoring autophagic degradation of p62/SQSTM1. Methods Enzymol. 452, 181-97 (2009).
    • (2009) Methods Enzymol. , vol.452 , pp. 181-197
    • Bjorkoy, G.1
  • 32
    • 0028596526 scopus 로고
    • The methylotrophic yeast Hansenula polymorpha contains an inducible import pathway for peroxisomal matrix proteins with an N-terminal targeting signal (PTS2 proteins)
    • Faber, K. N. et al. The methylotrophic yeast Hansenula polymorpha contains an inducible import pathway for peroxisomal matrix proteins with an N-terminal targeting signal (PTS2 proteins). Proc. Natl. Acad. Sci. U. S. A. 91, 12985-9 (1994).
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 12985-12989
    • Faber, K.N.1
  • 34
    • 77950470469 scopus 로고    scopus 로고
    • Molecular mechanism and physiological role of pexophagy
    • Manjithaya, R., Nazarko, T. Y., Farré, J.-C. & Subramani, S. Molecular mechanism and physiological role of pexophagy. FEBS lett. 584, 1367-1373 (2010).
    • (2010) FEBS Lett. , vol.584 , pp. 1367-1373
    • Manjithaya, R.1    Nazarko, T.Y.2    Farré, J.-C.3    Subramani, S.4
  • 35
    • 61949387423 scopus 로고    scopus 로고
    • Biochemical methods to monitor autophagy-related processes in yeast
    • Cheong, H. & Klionsky, D. J. Biochemical methods to monitor autophagy-related processes in yeast. Methods Enzymol. 451, 1-26 (2008).
    • (2008) Methods Enzymol. , vol.451 , pp. 1-26
    • Cheong, H.1    Klionsky, D.J.2
  • 36
    • 0242403270 scopus 로고    scopus 로고
    • The role of nitrate reductase in the regulation of the nitrate assimilation pathway in the yeast Hansenula polymorpha
    • Navarro, F. J. et al. The role of nitrate reductase in the regulation of the nitrate assimilation pathway in the yeast Hansenula polymorpha. FEMS Yeast Res. 4, 149-55 (2003).
    • (2003) FEMS Yeast Res. , vol.4 , pp. 149-155
    • Navarro, F.J.1
  • 37
    • 0030005367 scopus 로고    scopus 로고
    • The genes YNI1 and YNR1, encoding nitrite reductase and nitrate reductase respectively in the yeast Hansenula polymorpha, are clustered and co-ordinately regulated
    • Brito, N., Avila, J., Perez, M. D., Gonzalez, C. & Siverio, J. M. The genes YNI1 and YNR1, encoding nitrite reductase and nitrate reductase respectively in the yeast Hansenula polymorpha, are clustered and co-ordinately regulated. Biochem. J. 317, 89-95 (1996).
    • (1996) Biochem. J. , vol.317 , pp. 89-95
    • Brito, N.1    Avila, J.2    Perez, M.D.3    Gonzalez, C.4    Siverio, J.M.5
  • 38
    • 0030095876 scopus 로고    scopus 로고
    • Identification in vitro of a post-translational regulatory site in the hinge 1 region of Arabidopsis nitrate reductase
    • Su, W., Huber, S. C. & Crawford, N. M. Identification in vitro of a post-translational regulatory site in the hinge 1 region of Arabidopsis nitrate reductase. Plant Cell 8, 519-27 (1996).
    • (1996) Plant Cell , vol.8 , pp. 519-527
    • Su, W.1    Huber, S.C.2    Crawford, N.M.3
  • 39
    • 0034060414 scopus 로고    scopus 로고
    • Discrepancy between nitrate reduction rates in intact leaves and nitrate reductase activity in leaf extracts: What limits nitrate reduction in situ?
    • Kaiser, W. M., Kandlbinder, A., Stoimenova, M. & Glaab, J. Discrepancy between nitrate reduction rates in intact leaves and nitrate reductase activity in leaf extracts: what limits nitrate reduction in situ? Planta 210, 801-7 (2000).
    • (2000) Planta , vol.210 , pp. 801-807
    • Kaiser, W.M.1    Kandlbinder, A.2    Stoimenova, M.3    Glaab, J.4
  • 40
  • 41
    • 33947100511 scopus 로고    scopus 로고
    • Are nitrate concentrations in leafy vegetables within safe limits?
    • Umar, S., Iqbal, M. & Abrol, Y. Are nitrate concentrations in leafy vegetables within safe limits? Curr. sci. 92, 355-360 (2007).
    • (2007) Curr. Sci. , vol.92 , pp. 355-360
    • Umar, S.1    Iqbal, M.2    Abrol, Y.3
  • 42
    • 0040949996 scopus 로고
    • Effective of aerobic and anaerobic conditions on the invivo nitrate reductase assay in spinach leaves
    • Mann, A. F., Hucklesby, D. P. & Hewitt, E. J. Effective of aerobic and anaerobic conditions on the invivo nitrate reductase assay in spinach leaves. Planta 146, 83-89 (1979).
    • (1979) Planta , vol.146 , pp. 83-89
    • Mann, A.F.1    Hucklesby, D.P.2    Hewitt, E.J.3
  • 43
    • 0039699919 scopus 로고    scopus 로고
    • The activation state of nitrate reductase is not always correlated with total nitrate reductase activity in leaves
    • Man, H. M., Abd-El Baki, G. K., Stegmann, P., Weiner, H. & Kaiser, W. M. The activation state of nitrate reductase is not always correlated with total nitrate reductase activity in leaves. Planta 209, 462-8 (1999).
    • (1999) Planta , vol.209 , pp. 462-468
    • Man, H.M.1    Abd-El Baki, G.K.2    Stegmann, P.3    Weiner, H.4    Kaiser, W.M.5
  • 44
    • 13144273043 scopus 로고
    • Inactivation of nitrate reductase from wheat and rice leaves
    • Ramarao, C. S., Srinivasan & Naik, M. S. Inactivation of nitrate reductase from wheat and rice leaves. Phytochemistry 20, 1487-1491 (1981).
    • (1981) Phytochemistry , vol.20 , pp. 1487-1491
    • Ramarao, C.S.1    Srinivasan2    Naik, M.S.3
  • 45
    • 0025719504 scopus 로고
    • Transformation system for an asporogenous methylotrophic yeast Candida boidinii: Cloning of the orotidine-59-phosphate decarboxylase gene (URA3) isolation of uracil auxotrophic mutants and use of the mutants for integrative transformation
    • Sakai, Y., Kazarimoto, T. & Tani, Y. Transformation system for an asporogenous methylotrophic yeast, Candida boidinii: cloning of the orotidine-59-phosphate decarboxylase gene (URA3), isolation of uracil auxotrophic mutants, and use of the mutants for integrative transformation. J. Bacteriol. 173, 7458-7463 (1991).
    • (1991) J. Bacteriol. , vol.173 , pp. 7458-7463
    • Sakai, Y.1    Kazarimoto, T.2    Tani, Y.3
  • 46
    • 34547652261 scopus 로고    scopus 로고
    • Gene-tagging mutagenesis in the methylotrophic yeast Candida boidinii
    • Sasano, Y., Yurimoto, H. & Sakai, Y. Gene-tagging mutagenesis in the methylotrophic yeast Candida boidinii. J. Biosci. Bioeng. 104, 86-9 (2007).
    • (2007) J. Biosci. Bioeng. , vol.104 , pp. 86-89
    • Sasano, Y.1    Yurimoto, H.2    Sakai, Y.3
  • 47
    • 0027315207 scopus 로고
    • High-frequency transformation of a methylotrophic yeast, Candida boidinii, with autonomously replicating plasmids which are also functional in Saccharomyces cerevisiae
    • Sakai, Y., Goh, T. & Tani, Y. High-frequency transformation of a methylotrophic yeast, Candida boidinii, with autonomously replicating plasmids which are also functional in Saccharomyces cerevisiae. J. Bacteriol. 175, 3556-3562 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 3556-3562
    • Sakai, Y.1    Goh, T.2    Tani, Y.3
  • 48
    • 0026697675 scopus 로고
    • Directed mutagenesis in an asporogenous methylotrophic yeast: Cloning, sequencing, and one-step gene disruption of the 3-isopropylmalate dehydrogenase gene (LEU2) of Candida boidinii to derive doubly auxotrophic marker strains
    • Sakai, Y. & Tani, Y. Directed mutagenesis in an asporogenous methylotrophic yeast: cloning, sequencing, and one-step gene disruption of the 3-isopropylmalate dehydrogenase gene (LEU2) of Candida boidinii to derive doubly auxotrophic marker strains. J. Bacteriol. 174, 5988-5993 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 5988-5993
    • Sakai, Y.1    Tani, Y.2
  • 49
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-54 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 50
    • 62849119350 scopus 로고    scopus 로고
    • Characterization and expression analysis of a gene cluster for nitrate assimilation from the yeast Arxula adeninivorans
    • Boer, E., Schroter, A., Bode, R., Piontek, M. & Kunze, G. Characterization and expression analysis of a gene cluster for nitrate assimilation from the yeast Arxula adeninivorans. Yeast 26, 83-93 (2009).
    • (2009) Yeast , vol.26 , pp. 83-93
    • Boer, E.1    Schroter, A.2    Bode, R.3    Piontek, M.4    Kunze, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.