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Volumn 4, Issue , 2011, Pages 13-19

Analysis of the membrane proteins of an Antarctic bacterium Pseudomonas syringae

Author keywords

Integral membrane proteins; Membrane proteins; Subcellular localization; Trans membrane domains

Indexed keywords


EID: 84896742009     PISSN: None     EISSN: 11786418     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (2)

References (37)
  • 1
    • 0035106351 scopus 로고    scopus 로고
    • Large scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn MP, Wolters D, Yates JR. Large scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol. 2001;19:242-47.
    • (2001) Nat Biotechnol. , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 2
    • 0038561131 scopus 로고    scopus 로고
    • A method for the comprehensive proteomic analysis of membrane proteins
    • Wu CC, MacCoss MJ, Howell KE, Yates JR. A method for the comprehensive proteomic analysis of membrane proteins. Nat Biotechnol. 2003;21:532-38.
    • (2003) Nat Biotechnol. , vol.21 , pp. 532-538
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Yates, J.R.4
  • 3
    • 0037370373 scopus 로고    scopus 로고
    • Proteomics: the first decade and beyond
    • Patterson SD, Abersold RH. Proteomics: the first decade and beyond. Nat Genet. 2003;33:311-23.
    • (2003) Nat Genet. , vol.33 , pp. 311-323
    • Patterson, S.D.1    Abersold, R.H.2
  • 4
    • 0031568420 scopus 로고    scopus 로고
    • Direct analysis and identification of proteins in mixtures by LC/MS/MS and database searching at the low-femtomole level
    • McCormack AL, Schieltz DM, Goode B, et al. Direct analysis and identification of proteins in mixtures by LC/MS/MS and database searching at the low-femtomole level. Anal Chem. 1997;69:767-76.
    • (1997) Anal Chem. , vol.69 , pp. 767-776
    • McCormack, A.L.1    Schieltz, D.M.2    Goode, B.3
  • 5
    • 59249084983 scopus 로고    scopus 로고
    • Identification of proteins from membrane preparations by a combination of MALDI TOF/TOF and LC coupled ion trap MS analysis of an Antarctic bacterium Pseudomonas syringae Lz4W, a strain with unsequenced genome
    • Jagannadham MV. Identification of proteins from membrane preparations by a combination of MALDI TOF/TOF and LC coupled ion trap MS analysis of an Antarctic bacterium Pseudomonas syringae Lz4W, a strain with unsequenced genome. Electrophoresis. 2008;29:4341-50.
    • (2008) Electrophoresis. , vol.29 , pp. 4341-4350
    • Jagannadham, M.V.1
  • 6
    • 79958017231 scopus 로고    scopus 로고
    • Identification of outer membrane proteins from an Antarctic bacterium
    • First Published on March 29, doi:10.1074/mcp. M110.004549 (In Press).
    • Jagannadham MV, Abou-Eladab EF, Kulkarni HM. Identification of outer membrane proteins from an Antarctic bacterium. Pseudomonas syringae Lz4W. M110.004549. First Published on March 29, 2011, doi:10.1074/mcp. M110.004549 (In Press).
    • (2011) Pseudomonas syringae Lz4W. M110.004549
    • Jagannadham, M.V.1    Abou-Eladab, E.F.2    Kulkarni, H.M.3
  • 7
    • 0034630358 scopus 로고    scopus 로고
    • Two dimensional electrophoresis of membrane proteins using immobilized pH gradients
    • Molloy MP. Two dimensional electrophoresis of membrane proteins using immobilized pH gradients. Anal Biochem. 2000;280:831-40.
    • (2000) Anal Biochem. , vol.280 , pp. 831-840
    • Molloy, M.P.1
  • 8
    • 69249222678 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: love is possible, but so difficult
    • Rabilloud T. Membrane proteins and proteomics: love is possible, but so difficult. Electrophoresis. 2009;30:S174-80.
    • (2009) Electrophoresis. , vol.30
    • Rabilloud, T.1
  • 9
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: un amour impossible?
    • Santoni V, Molloy MP, Rabilloud T. Membrane proteins and proteomics: un amour impossible? Electrophoresis. 2000;21:1054-70.
    • (2000) Electrophoresis. , vol.21 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.P.2    Rabilloud, T.3
  • 10
    • 0028061982 scopus 로고
    • Microbial fatty acids and thermal adaptation
    • Suitari M, Laakso S. Microbial fatty acids and thermal adaptation. Crit Rev Microbiol. 1994;20:285-328.
    • (1994) Crit Rev Microbiol. , vol.20 , pp. 285-328
    • Suitari, M.1    Laakso, S.2
  • 11
    • 1842509102 scopus 로고    scopus 로고
    • Psychrophilic enzymes: hot topics in cold adaptation
    • Feller G, Gerdy C. Psychrophilic enzymes: hot topics in cold adaptation. Nature Mocrobiol Rev. 2003;1:200-8.
    • (2003) Nature Mocrobiol Rev. , vol.1 , pp. 200-208
    • Feller, G.1    Gerdy, C.2
  • 12
    • 0026353349 scopus 로고
    • The major carotenoid pigment of a Psychrotrophic Micrococcus roseus: purification, structure and interaction of the pigment with synthetic membranes
    • Jagannadham MV, Jayathirtha Rao V, Shivaji S. The major carotenoid pigment of a Psychrotrophic Micrococcus roseus: purification, structure and interaction of the pigment with synthetic membranes. J Bacteriol. 1991; 173:7911-17.
    • (1991) J Bacteriol. , vol.173 , pp. 7911-7917
    • Jagannadham, M.V.1    Jayathirtha Rao, V.2    Shivaji, S.3
  • 13
    • 0030000233 scopus 로고    scopus 로고
    • The major carotenoid pigment of a psychrotrophic Micrococcus roseuss train:fluorescence properties of the pigment and its binding to membranes
    • Jagannadham MV, Chattopadhyay MK, Shivaji S. The major carotenoid pigment of a psychrotrophic Micrococcus roseuss train:fluorescence properties of the pigment and its binding to membranes. Biochem Biophys Res Commun. 1996;220:724-28.
    • (1996) Biochem Biophys Res Commun. , vol.220 , pp. 724-728
    • Jagannadham, M.V.1    Chattopadhyay, M.K.2    Shivaji, S.3
  • 14
    • 0030567962 scopus 로고    scopus 로고
    • In vivo characteristics and localization of carotenoid pigments in psychrotrophic and mesophilic Micrococcus roseus using photoaccoustic spectroscopy
    • Jagannadham MV, Narayanan K, Mohan Rao C, Shivaji S. In vivo characteristics and localization of carotenoid pigments in psychrotrophic and mesophilic Micrococcus roseus using photoaccoustic spectroscopy. Biochem Biophys Res Commun. 1996;227:221-26.
    • (1996) Biochem Biophys Res Commun. , vol.227 , pp. 221-226
    • Jagannadham, M.V.1    Narayanan, K.2    Mohan Rao, C.3    Shivaji, S.4
  • 15
    • 0031561423 scopus 로고    scopus 로고
    • Carotenoid pigments of an Antarctic bacterium Micrococcus roseus: temperature dependent biosynthesis, structure and interection with synthetic membranes
    • Chattopadhyay MK, Jagannadham MV, Vairamani M, Shivaji S. Carotenoid pigments of an Antarctic bacterium Micrococcus roseus: temperature dependent biosynthesis, structure and interection with synthetic membranes. Biochem Bipohys Res Commun. 1997;239:85-90.
    • (1997) Biochem Bipohys Res Commun. , vol.239 , pp. 85-90
    • Chattopadhyay, M.K.1    Jagannadham, M.V.2    Vairamani, M.3    Shivaji, S.4
  • 16
    • 0034131142 scopus 로고    scopus 로고
    • Caratonoids of an Antarctic psychrotolerant bacterium Spingobacteriumantarcticus and a mesophilic bacterium Spingobacteriummultivorum
    • Jagannadham MV, Chattopadhyay MK, Subbalakshmi C, et al. Caratonoids of an Antarctic psychrotolerant bacterium Spingobacteriumantarcticus and a mesophilic bacterium Spingobacteriummultivorum. Arch Microbiol. 2000; 173:418-23.
    • (2000) Arch Microbiol. , vol.173 , pp. 418-423
    • Jagannadham, M.V.1    Chattopadhyay, M.K.2    Subbalakshmi, C.3
  • 17
    • 0028608786 scopus 로고
    • Phosphorylation of membrane proteins in response to temperature in an Antarctic Pseudomonas syringae
    • Ray MK, Kumar GS, Shivaji S. Phosphorylation of membrane proteins in response to temperature in an Antarctic Pseudomonas syringae. Microbiology. 1994;140:3217-23.
    • (1994) Microbiology. , vol.140 , pp. 3217-3223
    • Ray, M.K.1    Kumar, G.S.2    Shivaji, S.3
  • 18
    • 0033043956 scopus 로고    scopus 로고
    • Studies on the cytoplasmic protein tyrosine kinase activity of the Antarctic bacterium Pseudomonas syringae
    • Jagatap P, Ray MK. Studies on the cytoplasmic protein tyrosine kinase activity of the Antarctic bacterium Pseudomonas syringae. FEMS Micro Biol Lett. 1999;173:379-88.
    • (1999) FEMS Micro Biol Lett. , vol.173 , pp. 379-388
    • Jagatap, P.1    Ray, M.K.2
  • 19
    • 0041462889 scopus 로고    scopus 로고
    • Prpteomic analysis of the Escherichia coli outer membrane
    • Molloy MP, Herbert BR, Slade MB, et al. Prpteomic analysis of the Escherichia coli outer membrane. Eur J Biochem. 2000;267:2871-81.
    • (2000) Eur J Biochem. , vol.267 , pp. 2871-2881
    • Molloy, M.P.1    Herbert, B.R.2    Slade, M.B.3
  • 20
    • 0028204136 scopus 로고
    • Isolation and characterization of outer membrane proteins of Burkholderia (Pseudomonas) pseudomonalli
    • Gotoh N, White NJ, Chowagal W, Woods DE. Isolation and characterization of outer membrane proteins of Burkholderia (Pseudomonas) pseudomonalli. Microbiology. 1994;140:797-805.
    • (1994) Microbiology. , vol.140 , pp. 797-805
    • Gotoh, N.1    White, N.J.2    Chowagal, W.3    Woods, D.E.4
  • 21
    • 77954199597 scopus 로고    scopus 로고
    • PSORTb 3.0; improved protein subcellular localization prediction with refined localization sub categories and predictive capabilities for all prokaryotes
    • Yu NY, Wagner JR, Liard MR, et al. PSORTb 3.0; improved protein subcellular localization prediction with refined localization sub categories and predictive capabilities for all prokaryotes. Bioinformatics. 2010;26: 1608-15.
    • (2010) Bioinformatics. , vol.26 , pp. 1608-1615
    • Yu, N.Y.1    Wagner, J.R.2    Liard, M.R.3
  • 22
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • Tusnady GE, Simon I. The HMMTOP transmembrane topology prediction server. Bioinformatics. 2001;17:849-50.
    • (2001) Bioinformatics. , vol.17 , pp. 849-850
    • Tusnady, G.E.1    Simon, I.2
  • 23
    • 3042579686 scopus 로고    scopus 로고
    • Best alpha-helical transmembrane protein topology predictions are achieved using hidden MARKOV models and evolutionary information
    • Viklund H, Elofsson A. Best alpha-helical transmembrane protein topology predictions are achieved using hidden MARKOV models and evolutionary information. Protein Sci. 2004;13:1980-17.
    • (2004) Protein Sci. , vol.13 , pp. 1917-1980
    • Viklund, H.1    Elofsson, A.2
  • 24
    • 15844431346 scopus 로고    scopus 로고
    • PSORTb 2.0: expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis
    • Gardy JL, et al. PSORTb 2.0: expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis. Bioinformatics. 2005;21:617-23.
    • (2005) Bioinformatics. , vol.21 , pp. 617-623
    • Gardy, J.L.1
  • 25
    • 3242879514 scopus 로고    scopus 로고
    • BOMP: a program to predict integral β-barrel outer membrane proteins encoded within genomes of Gram-negative bacteria
    • Berven FS, Flikka K, Jensen HB, Eidhammer I. BOMP: a program to predict integral β-barrel outer membrane proteins encoded within genomes of Gram-negative bacteria. Nucleic Acid Res. 2004;32:W394-9.
    • (2004) Nucleic Acid Res. , vol.32
    • Berven, F.S.1    Flikka, K.2    Jensen, H.B.3    Eidhammer, I.4
  • 26
    • 0025976068 scopus 로고
    • Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein
    • Struyve M, Moons M, Tommassen J. Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein. J Mol Biol. 1991;218:141-8.
    • (1991) J Mol Biol. , vol.218 , pp. 141-148
    • Struyve, M.1    Moons, M.2    Tommassen, J.3
  • 27
    • 0036147641 scopus 로고    scopus 로고
    • Towards genomic identification of beta-barrel membrane proteins: composition and architecture of known structures
    • Wimley CW. Towards genomic identification of beta-barrel membrane proteins: composition and architecture of known structures. Protein Sci. 2002;11:301-12.
    • (2002) Protein Sci. , vol.11 , pp. 301-312
    • Wimley, C.W.1
  • 28
    • 25444484398 scopus 로고    scopus 로고
    • TMB-Hunt: an amino acid composition based method to screen proteomes for beta-barrel trans membrane proteins
    • Garrow AG, Agnew A, Westhead DR. TMB-Hunt: an amino acid composition based method to screen proteomes for beta-barrel trans membrane proteins. BMC Bioinformatics. 2005;6:56.
    • (2005) BMC Bioinformatics. , vol.6 , pp. 56
    • Garrow, A.G.1    Agnew, A.2    Westhead, D.R.3
  • 29
    • 0031614678 scopus 로고    scopus 로고
    • A hidden Markov model for predicting transmembrane helices in protein sequences
    • Glasgow J, Littlejohn T, Major FR. Lathrop R, SankoffDC, Sensen CM, editors. P. CA: AAAI Press
    • Sonnhammer ELL, von Heijne G, Krogh A. "A hidden Markov model for predicting transmembrane helices in protein sequences". In: Glasgow J, Littlejohn T, Major FR. Lathrop R, SankoffDC, Sensen CM, editors. Proc of Sixth Int Conf on Intelligent Systems for Molecular Biology. P. CA: AAAI Press; 1998:175-182.
    • (1998) Proc of Sixth Int Conf on Intelligent Systems for Molecular Biology , pp. 175-182
    • Sonnhammer, E.L.L.1    von Heijne, G.2    Krogh, A.3
  • 30
    • 0034724567 scopus 로고    scopus 로고
    • High resolution structure of the OmpA membrane domain
    • Pautsch A, Schulz GE. High resolution structure of the OmpA membrane domain. J Mol Biol. 2000;298:273-82.
    • (2000) J Mol Biol. , vol.298 , pp. 273-282
    • Pautsch, A.1    Schulz, G.E.2
  • 31
    • 33847292794 scopus 로고    scopus 로고
    • beta-barrel membrane bacterial proteins: structure, function, assembly and interaction with lipids
    • Galdiero S, Galdiero M, Pedone C. beta-barrel membrane bacterial proteins: structure, function, assembly and interaction with lipids. Current protein pept Sci. 2007;8:63-82.
    • (2007) Current protein pept Sci. , vol.8 , pp. 63-82
    • Galdiero, S.1    Galdiero, M.2    Pedone, C.3
  • 32
    • 64049114180 scopus 로고    scopus 로고
    • Evaluation of procedures for outermembrane isolation from Campylobacter jejuni
    • Hobb RL, Fields JA, Burns CM, Thompson SA. Evaluation of procedures for outermembrane isolation from Campylobacter jejuni. Micribiology. 2009;155(Pt 3):979-88.
    • (2009) Micribiology. , vol.155 , Issue.PART 3 , pp. 979-988
    • Hobb, R.L.1    Fields, J.A.2    Burns, C.M.3    Thompson, S.A.4
  • 33
    • 78649833943 scopus 로고    scopus 로고
    • Efficient sub fractionation of Gram-negative bacteria proteomics studies
    • Thein M, Souer G, Paramasivam N, Grin I, Linke D. Efficient sub fractionation of Gram-negative bacteria proteomics studies. J Proteome Res. 2010;9:6135-47.
    • (2010) J Proteome Res. , vol.9 , pp. 6135-6147
    • Thein, M.1    Souer, G.2    Paramasivam, N.3    Grin, I.4    Linke, D.5
  • 34
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane topology with a hidden Markov model: application to complete genomes
    • Krogh A, Larsson B, Von Heijne G, Sonnhammer ELL. Predicting transmembrane topology with a hidden Markov model: application to complete genomes. J Mol Biol. 2001;305:567-80.
    • (2001) J Mol Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4
  • 35
    • 31344476293 scopus 로고    scopus 로고
    • Low temperature induced systems failure in Escherichia coli: insights from rescue by cold adapted chaperons
    • Strocchi M, Ferrer M, Timmis KN, Golyshin PN. Low temperature induced systems failure in Escherichia coli: insights from rescue by cold adapted chaperons. Proteomics. 2006;6:193-206.
    • (2006) Proteomics. , vol.6 , pp. 193-206
    • Strocchi, M.1    Ferrer, M.2    Timmis, K.N.3    Golyshin, P.N.4
  • 36
    • 77956226824 scopus 로고    scopus 로고
    • Aspartate amino transferase is involved in cold adaptation in psychrophillic Pseudomonas syringae
    • Sundereswaran VR, Singh AK, Dube S, Shivaji S. Aspartate amino transferase is involved in cold adaptation in psychrophillic Pseudomonas syringae. Arch Microbiol. 2010;192:663-72.
    • (2010) Arch Microbiol. , vol.192 , pp. 663-672
    • Sundereswaran, V.R.1    Singh, A.K.2    Dube, S.3    Shivaji, S.4
  • 37
    • 33645697736 scopus 로고    scopus 로고
    • Mechanism of bacterial adaptation to low temperature
    • Chattopadhyay MK. Mechanism of bacterial adaptation to low temperature. J Biosci. 2006;3:157-65.
    • (2006) J Biosci. , vol.3 , pp. 157-165
    • Chattopadhyay, M.K.1


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