메뉴 건너뛰기




Volumn 75, Issue 8, 2012, Pages 2488-2499

Differential expression of membrane proteins helps Antarctic Pseudomonas syringae to acclimatize upon temperature variations

Author keywords

Acclimatization; Antarctic bacterium; Cold adaptation; LC ESI MS MS; MALDI TOF TOF; Membrane proteins

Indexed keywords

AMIDOSULFOBETAINE; BETAINE; DETERGENT; MEMBRANE PROTEIN; SUCROSE; UNCLASSIFIED DRUG;

EID: 84859265363     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.02.033     Document Type: Article
Times cited : (15)

References (46)
  • 1
    • 0031788886 scopus 로고    scopus 로고
    • Adaptation to low temperature and regulation of gene expression in Antarctic psychrotrophic bacteria
    • Ray M.K., Kumar G.S., Janiyani K., Kannan K., Jagtap P., Basu M.K., et al. Adaptation to low temperature and regulation of gene expression in Antarctic psychrotrophic bacteria. J Biosci 1998, 23:423-435.
    • (1998) J Biosci , vol.23 , pp. 423-435
    • Ray, M.K.1    Kumar, G.S.2    Janiyani, K.3    Kannan, K.4    Jagtap, P.5    Basu, M.K.6
  • 2
    • 0042410702 scopus 로고    scopus 로고
    • Temperature effects on biological systems: introduction
    • Rowbury R.J. Temperature effects on biological systems: introduction. Sci Prog 2003, 86(pt 1-2):1-7.
    • (2003) Sci Prog , vol.86 , Issue.1-2 PART , pp. 1-7
    • Rowbury, R.J.1
  • 3
    • 0031786750 scopus 로고
    • Does membranes physical state control the expression of heat shock and other genes?
    • Vigh L., Maresca B., Harwood J.L. Does membranes physical state control the expression of heat shock and other genes?. Trends Biochem Sci 1993, 23:369-374.
    • (1993) Trends Biochem Sci , vol.23 , pp. 369-374
    • Vigh, L.1    Maresca, B.2    Harwood, J.L.3
  • 4
    • 0031795752 scopus 로고    scopus 로고
    • Lipid polymorphism and protein-lipid interactions
    • Epand R.M. Lipid polymorphism and protein-lipid interactions. Biochim Biophys Acta 1998, 1376:353-368.
    • (1998) Biochim Biophys Acta , vol.1376 , pp. 353-368
    • Epand, R.M.1
  • 5
    • 0028081744 scopus 로고
    • Adaptation of Pseudomonas putida S12 to ethanol and toluene at the level of fatty acid composition of membranes
    • Heipieper H.J., de Bont J.A. Adaptation of Pseudomonas putida S12 to ethanol and toluene at the level of fatty acid composition of membranes. Appl Environ Microbiol 1994, 60:4440-4444.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 4440-4444
    • Heipieper, H.J.1    de Bont, J.A.2
  • 6
    • 0019874168 scopus 로고
    • Dynamic states of phospholipids in Escherichia coli B membrane. Electron spin resonance studies with biosynthetically generated phospholipid spin labels
    • Takeuchi Y., Ohnishi S.I., Ishinaga M., Kito M. Dynamic states of phospholipids in Escherichia coli B membrane. Electron spin resonance studies with biosynthetically generated phospholipid spin labels. Biochim Biophys Acta 1981, 646:119-125.
    • (1981) Biochim Biophys Acta , vol.646 , pp. 119-125
    • Takeuchi, Y.1    Ohnishi, S.I.2    Ishinaga, M.3    Kito, M.4
  • 7
    • 0031561423 scopus 로고    scopus 로고
    • Carotenoid pigments of an Antarctic psychrotrophic bacterium Micrococcus roseus: temperature dependent biosynthesis, structure, and interaction with synthetic membranes
    • Chattopadhyay M.K., Jagannadham M.V., Vairamani M., Shivaji S. Carotenoid pigments of an Antarctic psychrotrophic bacterium Micrococcus roseus: temperature dependent biosynthesis, structure, and interaction with synthetic membranes. Biochem Biophys Res Commun 1997, 239:85-90.
    • (1997) Biochem Biophys Res Commun , vol.239 , pp. 85-90
    • Chattopadhyay, M.K.1    Jagannadham, M.V.2    Vairamani, M.3    Shivaji, S.4
  • 8
    • 0030000233 scopus 로고    scopus 로고
    • The major carotenoid pigment of a psychrotrophic Micrococcus roseus strain: fluorescence properties of the pigment and its binding to membranes
    • Jagannadham M.V., Chattopadhyay M.K., Shivaji S. The major carotenoid pigment of a psychrotrophic Micrococcus roseus strain: fluorescence properties of the pigment and its binding to membranes. Biochem Biophys Res Commun 1996, 220:724-728.
    • (1996) Biochem Biophys Res Commun , vol.220 , pp. 724-728
    • Jagannadham, M.V.1    Chattopadhyay, M.K.2    Shivaji, S.3
  • 9
    • 0030567962 scopus 로고    scopus 로고
    • In vivo characteristics and localisation of carotenoid pigments in psychrotrophic and mesophilic Micrococcus roseus using photoacoustic spectroscopy
    • Jagannadham M.V., Narayanan K., Rao C.M., Shivaji S. In vivo characteristics and localisation of carotenoid pigments in psychrotrophic and mesophilic Micrococcus roseus using photoacoustic spectroscopy. Biochem Biophys Res Commun 1996, 227:221-226.
    • (1996) Biochem Biophys Res Commun , vol.227 , pp. 221-226
    • Jagannadham, M.V.1    Narayanan, K.2    Rao, C.M.3    Shivaji, S.4
  • 10
    • 0034131142 scopus 로고    scopus 로고
    • Carotenoids of an Antarctic psychrotolerant bacterium, Sphingobacterium antarcticus, and a mesophilic bacterium, Sphingobacterium multivorum
    • Jagannadham M.V., Chattopadhyay M.K., Subbalakshmi C., Vairamani M., Narayanan K., Rao C.M., et al. Carotenoids of an Antarctic psychrotolerant bacterium, Sphingobacterium antarcticus, and a mesophilic bacterium, Sphingobacterium multivorum. Arch Microbiol 2000, 173:418-424.
    • (2000) Arch Microbiol , vol.173 , pp. 418-424
    • Jagannadham, M.V.1    Chattopadhyay, M.K.2    Subbalakshmi, C.3    Vairamani, M.4    Narayanan, K.5    Rao, C.M.6
  • 11
    • 0026353349 scopus 로고
    • The major carotenoid pigment of a psychrotrophic Micrococcus roseus strain: purification, structure, and interaction with synthetic membranes
    • Jagannadham M.V., Rao V.J., Shivaji S. The major carotenoid pigment of a psychrotrophic Micrococcus roseus strain: purification, structure, and interaction with synthetic membranes. J Bacteriol 1991, 173:7911-7917.
    • (1991) J Bacteriol , vol.173 , pp. 7911-7917
    • Jagannadham, M.V.1    Rao, V.J.2    Shivaji, S.3
  • 12
    • 0031608378 scopus 로고    scopus 로고
    • Molecular adaptations in psychrophillic bacteria: potential biotechnological applications
    • Russell N.J. Molecular adaptations in psychrophillic bacteria: potential biotechnological applications. Adv Biochem Eng Biotechnol 1998, 61:1-21.
    • (1998) Adv Biochem Eng Biotechnol , vol.61 , pp. 1-21
    • Russell, N.J.1
  • 13
    • 0028061982 scopus 로고
    • Microbial fatty acids and thermal adaptation
    • Suutari 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
    • Suutari, M.1    Laakso, S.2
  • 14
    • 0033043956 scopus 로고    scopus 로고
    • Studies on the cytoplasmic protein tyrosine kinase activity of the Antarctic psychrotrophic bacterium Pseudomonas syringae
    • Jagtap P., Ray M.K. Studies on the cytoplasmic protein tyrosine kinase activity of the Antarctic psychrotrophic bacterium Pseudomonas syringae. FEMS Microbiol Lett 1999, 173:379-388.
    • (1999) FEMS Microbiol Lett , vol.173 , pp. 379-388
    • Jagtap, P.1    Ray, M.K.2
  • 15
    • 0028608786 scopus 로고
    • Phosphorylation of membrane proteins in response to temperature in an Antarctic Pseudomonas syringae
    • Ray M.K., Kumar G.S., Shivaji S. Phosphorylation of membrane proteins in response to temperature in an Antarctic Pseudomonas syringae. Microbiology 1994, 140:3217-3223.
    • (1994) Microbiology , vol.140 , pp. 3217-3223
    • Ray, M.K.1    Kumar, G.S.2    Shivaji, S.3
  • 16
    • 41949097802 scopus 로고    scopus 로고
    • Auxotrophy in natural isolate: minimal requirements for growth of the Antarctic psychrotrophic bacterium Pseudomonas syringae Lz4W
    • Sahu B., Ray M.K. Auxotrophy in natural isolate: minimal requirements for growth of the Antarctic psychrotrophic bacterium Pseudomonas syringae Lz4W. J Basic Microbiol 2008, 48:38-47.
    • (2008) J Basic Microbiol , vol.48 , pp. 38-47
    • Sahu, B.1    Ray, M.K.2
  • 17
    • 78649833943 scopus 로고    scopus 로고
    • Efficient sub fractionation of gram-negative bacteria for proteomics studies
    • Thein M., Sauer G., Paramasivam N., Grin I., Linke D. Efficient sub fractionation of gram-negative bacteria for proteomics studies. J Proteome Res 2010, 9:6135-6147.
    • (2010) J Proteome Res , vol.9 , pp. 6135-6147
    • Thein, M.1    Sauer, G.2    Paramasivam, N.3    Grin, I.4    Linke, D.5
  • 18
    • 79958017231 scopus 로고    scopus 로고
    • Identification of outer membrane proteins from an Antarctic bacterium Pseudomonas syringae Lz4W
    • Jagannadham M.V., Aobu-Eladab E.F., Kulkarni H.M. Identification of outer membrane proteins from an Antarctic bacterium Pseudomonas syringae Lz4W. Mol Cell Proteomics 2011, 10.1074/mcp.M110.004549.
    • (2011) Mol Cell Proteomics
    • Jagannadham, M.V.1    Aobu-Eladab, E.F.2    Kulkarni, H.M.3
  • 19
    • 33749242423 scopus 로고    scopus 로고
    • Profiling human brain proteome by multi-dimensional separations coupled with MS
    • Park Y.M., Kim J.Y., Kwon K.H., Lee S.K., Kim Y.H., Kim S.Y., et al. Profiling human brain proteome by multi-dimensional separations coupled with MS. Proteomics 2006, 6:4978-4986.
    • (2006) Proteomics , vol.6 , pp. 4978-4986
    • Park, Y.M.1    Kim, J.Y.2    Kwon, K.H.3    Lee, S.K.4    Kim, Y.H.5    Kim, S.Y.6
  • 20
    • 33645466243 scopus 로고    scopus 로고
    • Toward the complete membrane proteome: high coverage of integral membrane proteins through transmembrane peptide detection
    • Fischer F., Wolters D., Rogner M., Poetsch A. Toward the complete membrane proteome: high coverage of integral membrane proteins through transmembrane peptide detection. Mol Cell Proteomics 2006, 5:444-453.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 444-453
    • Fischer, F.1    Wolters, D.2    Rogner, M.3    Poetsch, A.4
  • 21
    • 33847681015 scopus 로고    scopus 로고
    • Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS
    • Zhang N., Chen R., Young N., Wishart D., Winter P., Weiner J.H., et al. Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS. Proteomics 2007, 7:484-493.
    • (2007) Proteomics , vol.7 , pp. 484-493
    • Zhang, N.1    Chen, R.2    Young, N.3    Wishart, D.4    Winter, P.5    Weiner, J.H.6
  • 22
    • 15844431346 scopus 로고    scopus 로고
    • PSORTb v. 2.0: expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis
    • Gardy J.L., Laird M.R., Chen F., Rey S., Walsh C.J., Ester M., et al. PSORTb v. 2.0: expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis. Bioinformatics 2005, 21:617-623.
    • (2005) Bioinformatics , vol.21 , pp. 617-623
    • Gardy, J.L.1    Laird, M.R.2    Chen, F.3    Rey, S.4    Walsh, C.J.5    Ester, M.6
  • 23
    • 0037347236 scopus 로고    scopus 로고
    • Evaluation of nonionic and zwitterionic detergents as membrane protein solubilizers in two-dimensional electrophoresis
    • Luche S., Santoni V., Rabilloud T. Evaluation of nonionic and zwitterionic detergents as membrane protein solubilizers in two-dimensional electrophoresis. Proteomics 2003, 3:249-253.
    • (2003) Proteomics , vol.3 , pp. 249-253
    • Luche, S.1    Santoni, V.2    Rabilloud, T.3
  • 24
    • 0033778077 scopus 로고    scopus 로고
    • Membrane proteomics: use of additive main effects with multiplicative interaction model to classify plasma membrane proteins according to their solubility and electrophoretic properties
    • Santoni V., Kieffer S., Desclaux D., Masson F., Rabilloud T. Membrane proteomics: use of additive main effects with multiplicative interaction model to classify plasma membrane proteins according to their solubility and electrophoretic properties. Electrophoresis 2000, 21:3329-3344.
    • (2000) Electrophoresis , vol.21 , pp. 3329-3344
    • Santoni, V.1    Kieffer, S.2    Desclaux, D.3    Masson, F.4    Rabilloud, T.5
  • 25
    • 0033673225 scopus 로고    scopus 로고
    • Complementing genomics with proteomics: the membrane subproteome of Pseudomonas aeruginosa PAO1
    • Nouwens A.S., Cordwell S.J., Larsen M.R., Molloy M.P., Gillings M., Willcox M.D., et al. Complementing genomics with proteomics: the membrane subproteome of Pseudomonas aeruginosa PAO1. Electrophoresis 2000, 21:3797-3809.
    • (2000) Electrophoresis , vol.21 , pp. 3797-3809
    • Nouwens, A.S.1    Cordwell, S.J.2    Larsen, M.R.3    Molloy, M.P.4    Gillings, M.5    Willcox, M.D.6
  • 26
    • 0036888989 scopus 로고    scopus 로고
    • Low-temperature-induced changes in composition and fluidity of lipopolysaccharides in the Antarctic psychrotrophic bacterium Pseudomonas syringae
    • Kumar G.S., Jagannadham M.V., Ray M.K. Low-temperature-induced changes in composition and fluidity of lipopolysaccharides in the Antarctic psychrotrophic bacterium Pseudomonas syringae. J Bacteriol 2002, 184:6746-6749.
    • (2002) J Bacteriol , vol.184 , pp. 6746-6749
    • Kumar, G.S.1    Jagannadham, M.V.2    Ray, M.K.3
  • 27
    • 59249084983 scopus 로고    scopus 로고
    • Identification of proteins from membrane preparations by a combination of MALDI TOF-TOF and LC-coupled linear ion trap MS analysis of an Antarctic bacterium Pseudomonas syringae Lz4W, a strain with unsequenced genome
    • Jagannadham M.V. Identification of proteins from membrane preparations by a combination of MALDI TOF-TOF and LC-coupled linear ion trap MS analysis of an Antarctic bacterium Pseudomonas syringae Lz4W, a strain with unsequenced genome. Electrophoresis 2008, 29:4341-4350.
    • (2008) Electrophoresis , vol.29 , pp. 4341-4350
    • Jagannadham, M.V.1
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0032961627 scopus 로고    scopus 로고
    • Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: a method for the removal of silver ions to enhance sensitivity
    • Gharahdaghi F., Weinberg C.R., Meagher D.A., Imai B.S., Mische S.M. Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: a method for the removal of silver ions to enhance sensitivity. Electrophoresis 1999, 20:601-605.
    • (1999) Electrophoresis , vol.20 , pp. 601-605
    • Gharahdaghi, F.1    Weinberg, C.R.2    Meagher, D.A.3    Imai, B.S.4    Mische, S.M.5
  • 33
    • 77954199597 scopus 로고    scopus 로고
    • PSORTb 3.0: improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes
    • Yu N.Y., Wagner J.R., Laird M.R., Melli G., Rey S., Lo R., et al. PSORTb 3.0: improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes. Bioinformatics 2010, 26:1608-1615.
    • (2010) Bioinformatics , vol.26 , pp. 1608-1615
    • Yu, N.Y.1    Wagner, J.R.2    Laird, M.R.3    Melli, G.4    Rey, S.5    Lo, R.6
  • 34
    • 33744471931 scopus 로고    scopus 로고
    • Enhanced automated function prediction using distantly related sequences and contextual association by PFP
    • Hawkins T., Luban S., Kihara D. Enhanced automated function prediction using distantly related sequences and contextual association by PFP. Protein Sci 2006, 15:1550-1556.
    • (2006) Protein Sci , vol.15 , pp. 1550-1556
    • Hawkins, T.1    Luban, S.2    Kihara, D.3
  • 35
    • 0030957650 scopus 로고    scopus 로고
    • Improvement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients
    • Rabilloud T., Adessi C., Giraudel A., Lunardi J. Improvement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis 1997, 18:307-316.
    • (1997) Electrophoresis , vol.18 , pp. 307-316
    • Rabilloud, T.1    Adessi, C.2    Giraudel, A.3    Lunardi, J.4
  • 36
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn M.P., Wolters D., Yates J.R. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol 2001, 19:242-247.
    • (2001) Nat Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 37
    • 0038561131 scopus 로고    scopus 로고
    • A method for the comprehensive proteomic analysis of membrane proteins
    • Wu C.C., MacCoss M.J., Howell K.E., Yates J.R. A method for the comprehensive proteomic analysis of membrane proteins. Nat Biotechnol 2003, 21:532-538.
    • (2003) Nat Biotechnol , vol.21 , pp. 532-538
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Yates, J.R.4
  • 38
    • 78650676710 scopus 로고    scopus 로고
    • Identifying the sequence and distinguishing the oxidized-methionine from phenylalanine peptides by MALDI TOF/TOF mass spectrometry in an Antarctic bacterium Pseudomonas syringae
    • Jagannadham M.V. Identifying the sequence and distinguishing the oxidized-methionine from phenylalanine peptides by MALDI TOF/TOF mass spectrometry in an Antarctic bacterium Pseudomonas syringae. Proteomics Insights 2009, 2:27-31.
    • (2009) Proteomics Insights , vol.2 , pp. 27-31
    • Jagannadham, M.V.1
  • 39
    • 79957980612 scopus 로고    scopus 로고
    • Acetylating tryptic peptides enhance b ion intensity in MALDI TOF/TOF: implications in peptide sequencing and identification of proteins in an Antarctic bacterium Pseudomonas syringae
    • Kulkarni H.M., Ramesh V., Srinivas R., Jagannadham M.V. Acetylating tryptic peptides enhance b ion intensity in MALDI TOF/TOF: implications in peptide sequencing and identification of proteins in an Antarctic bacterium Pseudomonas syringae. Proteomics Insights 2010, 3:1-16.
    • (2010) Proteomics Insights , vol.3 , pp. 1-16
    • Kulkarni, H.M.1    Ramesh, V.2    Srinivas, R.3    Jagannadham, M.V.4
  • 40
    • 31344476293 scopus 로고    scopus 로고
    • Low temperature-induced systems failure in Escherichia coli: insights from rescue by cold-adapted chaperones
    • Strocchi M., Ferrer M., Timmis K.N., Golyshin P.N. Low temperature-induced systems failure in Escherichia coli: insights from rescue by cold-adapted chaperones. 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
  • 41
    • 33645697736 scopus 로고    scopus 로고
    • Mechanism of bacterial adaptation to low temperature
    • Chattopadhyay M. Mechanism of bacterial adaptation to low temperature. J Biosci 2006, 31:157-165.
    • (2006) J Biosci , vol.31 , pp. 157-165
    • Chattopadhyay, M.1
  • 42
    • 0028198927 scopus 로고
    • Effect of growth temperatures on the protein levels in a psychrotrophic bacterium, Pseudomonas fragi
    • Hebraud M., Dubois E., Potier P., Labadie J. Effect of growth temperatures on the protein levels in a psychrotrophic bacterium, Pseudomonas fragi. J Bacteriol 1994, 176:4017-4024.
    • (1994) J Bacteriol , vol.176 , pp. 4017-4024
    • Hebraud, M.1    Dubois, E.2    Potier, P.3    Labadie, J.4
  • 45
    • 79955945455 scopus 로고    scopus 로고
    • Growth of Pseudomonas putida at low temperature: global transcriptomic and proteomic analyses
    • Fonseca P., Moreno R., Rojo F. Growth of Pseudomonas putida at low temperature: global transcriptomic and proteomic analyses. Env Microbiol Rep 2011, 3:329-339.
    • (2011) Env Microbiol Rep , vol.3 , pp. 329-339
    • Fonseca, P.1    Moreno, R.2    Rojo, F.3
  • 46
    • 76949084982 scopus 로고    scopus 로고
    • How do bacteria sense and respond to low temperatures?
    • Shivaji S., Prakash J.S.S. How do bacteria sense and respond to low temperatures?. Arch Microbiol 2010, 192:85-95.
    • (2010) Arch Microbiol , vol.192 , pp. 85-95
    • Shivaji, S.1    Prakash, J.S.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.