메뉴 건너뛰기




Volumn 10, Issue 7, 2011, Pages 3261-3273

Metabolic capabilities and systems fluctuations in haloarcula marismortui revealed by integrative genomics and proteomics analyses

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BACTERIAL PROTEIN; MEMBRANE PROTEIN;

EID: 79959967205     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr200290x     Document Type: Article
Times cited : (8)

References (47)
  • 2
    • 0017343306 scopus 로고
    • Physiology of halobacteriaceae
    • Dundas, I. E. Physiology of halobacteriaceae Adv. Microb. Physiol. 1977, 15, 85-120
    • (1977) Adv. Microb. Physiol. , vol.15 , pp. 85-120
    • Dundas, I.E.1
  • 4
    • 77953672648 scopus 로고    scopus 로고
    • Translation of Henrich Klebahn's 'Damaging agents of the klippfish - A contribution to the knowledge of the salt-loving organisms'
    • DasSarma, P.; Klebahn, G.; Klebahn, H. Translation of Henrich Klebahn's 'Damaging agents of the klippfish-a contribution to the knowledge of the salt-loving organisms' Saline Syst. 2010, 6, 7
    • (2010) Saline Syst. , vol.6 , pp. 7
    • Dassarma, P.1    Klebahn, G.2    Klebahn, H.3
  • 7
    • 44449095705 scopus 로고    scopus 로고
    • Genome sequences of Halobacterium species
    • DOI 10.1016/j.ygeno.2008.04.005, PII S088875430800092X
    • Ng, W. V.; Berquist, B. R.; Coker, J. A.; Capes, M.; Wu, T. H.; DasSarma, P.; DasSarma, S. Genome sequences of Halobacterium species Genomics 2008, 91 (6) 548-52 Author reply 553-4. (Pubitemid 351763874)
    • (2008) Genomics , vol.91 , Issue.6 , pp. 548-552
    • Ng, W.V.1    Berquist, B.R.2    Coker, J.A.3    Capes, M.4    Wu, T.H.5    DasSarma, P.6    DasSarma, S.7
  • 10
    • 25844454133 scopus 로고    scopus 로고
    • Living with two extremes: Conclusions from the genome sequence of Natronomonas pharaonis
    • DOI 10.1101/gr.3952905
    • Falb, M.; Pfeiffer, F.; Palm, P.; Rodewald, K.; Hickmann, V.; Tittor, J.; Oesterhelt, D. Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis Genome Res. 2005, 15 (10) 1336-43 (Pubitemid 41400899)
    • (2005) Genome Research , vol.15 , Issue.10 , pp. 1336-1343
    • Falb, M.1    Pfeiffer, F.2    Palm, P.3    Rodewald, K.4    Hickmann, V.5    Tittor, J.6    Oesterhelt, D.7
  • 13
    • 77956537114 scopus 로고    scopus 로고
    • Complete genome sequence of Halalkalicoccus jeotgali B3(T), an extremely halophilic archaeon
    • Roh, S. W.; Nam, Y. D.; Nam, S. H.; Choi, S. H.; Park, H. S.; Bae, J. W. Complete genome sequence of Halalkalicoccus jeotgali B3(T), an extremely halophilic archaeon J. Bacteriol. 2010, 192 (17) 4528-9
    • (2010) J. Bacteriol. , vol.192 , Issue.17 , pp. 4528-9
    • Roh, S.W.1    Nam, Y.D.2    Nam, S.H.3    Choi, S.H.4    Park, H.S.5    Bae, J.W.6
  • 14
    • 0034767491 scopus 로고    scopus 로고
    • Understanding the adaptation of Halobacterium species NRC-1 to its extreme environment through computational analysis of its genome sequence
    • DOI 10.1101/gr.190201
    • Kennedy, S. P.; Ng, W. V.; Salzberg, S. L.; Hood, L.; DasSarma, S. Understanding the adaptation of Halobacterium species NRC-1 to its extreme environment through computational analysis of its genome sequence Genome Res. 2001, 11 (10) 1641-50 (Pubitemid 33040491)
    • (2001) Genome Research , vol.11 , Issue.10 , pp. 1641-1650
    • Kennedy, S.P.1    Ng, W.V.2    Salzberg, S.L.3    Hood, L.4    DasSarma, S.5
  • 15
    • 0016139829 scopus 로고
    • Salt-dependent properties of proteins from extremely halophilic bacteria
    • Lanyi, J. K. Salt-dependent properties of proteins from extremely halophilic bacteria Bacteriol. Rev. 1974, 38 (3) 272-90
    • (1974) Bacteriol. Rev. , vol.38 , Issue.3 , pp. 272-90
    • Lanyi, J.K.1
  • 17
    • 0028806048 scopus 로고
    • Quantitative monitoring of gene expression patterns with a complementary DNA microarray
    • Schena, M.; Shalon, D.; Davis, R. W.; Brown, P. O. Quantitative monitoring of gene expression patterns with a complementary DNA microarray Science 1995, 270 (5235) 467-70
    • (1995) Science , vol.270 , Issue.5235 , pp. 467-70
    • Schena, M.1    Shalon, D.2    Davis, R.W.3    Brown, P.O.4
  • 18
    • 0026108692 scopus 로고
    • Light-directed, spatially addressable parallel chemical synthesis
    • Fodor, S. P.; Read, J. L.; Pirrung, M. C.; Stryer, L.; Lu, A. T.; Solas, D. Light-directed, spatially addressable parallel chemical synthesis Science 1991, 251 (4995) 767-73 (Pubitemid 21926165)
    • (1991) Science , vol.251 , Issue.4995 , pp. 767-773
    • Fodor, S.P.A.1    Read, J.L.2    Pirrung, M.C.3    Stryer, L.4    Lu, A.T.5    Solas, D.6
  • 20
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • DOI 10.1038/nature01511
    • Aebersold, R.; Mann, M. Mass spectrometry-based proteomics Nature 2003, 422 (6928) 198-207 (Pubitemid 36362757)
    • (2003) Nature , vol.422 , Issue.6928 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 21
    • 58149299336 scopus 로고    scopus 로고
    • Significance analysis of spectral count data in label-free shotgun proteomics
    • Choi, H.; Fermin, D.; Nesvizhskii, A. I. Significance analysis of spectral count data in label-free shotgun proteomics Mol. Cell. Proteomics 2008, 7 (12) 2373-85
    • (2008) Mol. Cell. Proteomics , vol.7 , Issue.12 , pp. 2373-85
    • Choi, H.1    Fermin, D.2    Nesvizhskii, A.I.3
  • 25
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • Oesterhelt, D.; Stoeckenius, W. Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane Methods Enzymol. 1974, 31 (Pt A) 667-78
    • (1974) Methods Enzymol. , vol.31 , Issue.PART A , pp. 667-78
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 26
    • 0031888036 scopus 로고    scopus 로고
    • High throughput protein characterization by automated reverse-phase chromatography/electrospray tandem mass spectrometry
    • Ducret, A.; Van Oostveen, I.; Eng, J. K.; Yates, J. R., 3rd; Aebersold, R. High throughput protein characterization by automated reverse-phase chromatography/electrospray tandem mass spectrometry Protein Sci. 1998, 7 (3) 706-19 (Pubitemid 28130893)
    • (1998) Protein Science , vol.7 , Issue.3 , pp. 706-719
    • Ducret, A.1    Van Oostveen, I.2    Eng, J.K.3    Yates III, J.R.4    Aebersold, R.5
  • 27
    • 0041834903 scopus 로고    scopus 로고
    • A microcapillary trap cartridge-microcapillary high-performance liquid chromatography electrospray ionization emitter device capable of peptide tandem mass spectrometry at the attomole level on an ion trap mass spectrometer with automated routine operation
    • Yi, E. C.; Lee, H.; Aebersold, R.; Goodlett, D. R. A microcapillary trap cartridge-microcapillary high-performance liquid chromatography electrospray ionization emitter device capable of peptide tandem mass spectrometry at the attomole level on an ion trap mass spectrometer with automated routine operation Rapid Commun. Mass Spectrom. 2003, 17 (18) 2093-8 (Pubitemid 37093085)
    • (2003) Rapid Communications in Mass Spectrometry , vol.17 , Issue.18 , pp. 2093-2098
    • Yi, E.C.1    Lee, H.2    Aebersold, R.3    Goodlett, D.R.4
  • 28
    • 33745977430 scopus 로고    scopus 로고
    • 5 by mass spectrometry and site-directed mutagenesis
    • DOI 10.1074/jbc.M601785200
    • Gao, Q.; Doneanu, C. E.; Shaffer, S. A.; Adman, E. T.; Goodlett, D. R.; Nelson, S. D. Identification of the interactions between cytochrome P450 2E1 and cytochrome b5 by mass spectrometry and site-directed mutagenesis J. Biol. Chem. 2006, 281 (29) 20404-17 (Pubitemid 44065814)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.29 , pp. 20404-20417
    • Gao, Q.1    Doneanu, C.E.2    Shaffer, S.A.3    Adman, E.T.4    Goodlett, D.R.5    Nelson, S.D.6
  • 30
    • 0029644596 scopus 로고
    • Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database
    • Yates, J. R., 3rd; Eng, J. K.; McCormack, A. L.; Schieltz, D. Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database Anal. Chem. 1995, 67 (8) 1426-36
    • (1995) Anal. Chem. , vol.67 , Issue.8 , pp. 1426-36
    • Yates III, J.R.1    Eng, J.K.2    McCormack, A.L.3    Schieltz, D.4
  • 31
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • DOI 10.1038/nmeth1019, PII NMETH1019
    • Elias, J. E.; Gygi, S. P. Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry Nat. Methods 2007, 4 (3) 207-14 (Pubitemid 46358868)
    • (2007) Nature Methods , vol.4 , Issue.3 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 32
    • 76149132007 scopus 로고    scopus 로고
    • Comparison of database search strategies for high precursor mass accuracy MS/MS data
    • Hsieh, E. J.; Hoopmann, M. R.; MacLean, B.; MacCoss, M. J. Comparison of database search strategies for high precursor mass accuracy MS/MS data J. Proteome Res 2010, 9 (2) 1138-43
    • (2010) J. Proteome Res , vol.9 , Issue.2 , pp. 1138-43
    • Hsieh, E.J.1    Hoopmann, M.R.2    MacLean, B.3    MacCoss, M.J.4
  • 33
    • 33746930864 scopus 로고    scopus 로고
    • A uniform proteomics MS/MS analysis platform utilizing open XML file formats
    • Keller, A.; Eng, J.; Zhang, N.; Li, X. J.; Aebersold, R. A uniform proteomics MS/MS analysis platform utilizing open XML file formats Mol. Syst. Biol. 2005, 1, 0017
    • (2005) Mol. Syst. Biol. , vol.1 , pp. 0017
    • Keller, A.1    Eng, J.2    Zhang, N.3    Li, X.J.4    Aebersold, R.5
  • 34
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • DOI 10.1021/ac0341261
    • Nesvizhskii, A. I.; Keller, A.; Kolker, E.; Aebersold, R. A statistical model for identifying proteins by tandem mass spectrometry Anal. Chem. 2003, 75 (17) 4646-58 (Pubitemid 37082259)
    • (2003) Analytical Chemistry , vol.75 , Issue.17 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 35
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • DOI 10.1021/ac025747h
    • Keller, A.; Nesvizhskii, A. I.; Kolker, E.; Aebersold, R. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search Anal. Chem. 2002, 74 (20) 5383-92 (Pubitemid 35215372)
    • (2002) Analytical Chemistry , vol.74 , Issue.20 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 37
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • DOI 10.1006/jmbi.2000.4315
    • Krogh, A.; Larsson, B.; von Heijne, G.; Sonnhammer, E. L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes J. Mol. Biol. 2001, 305 (3) 567-80 (Pubitemid 33032862)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4
  • 38
    • 0027932212 scopus 로고
    • Ketohexokinase (ATP:D-fructose 1-phosphotransferase) from a halophilic archaebacterium, Haloarcula vallismortis: Purification and properties
    • Rangaswamy, V.; Altekar, W. Ketohexokinase (ATP:D-fructose 1-phosphotransferase) from a halophilic archaebacterium, Haloarcula vallismortis: purification and properties J. Bacteriol. 1994, 176 (17) 5505-12 (Pubitemid 24273541)
    • (1994) Journal of Bacteriology , vol.176 , Issue.17 , pp. 5505-5512
    • Rangaswamy, V.1    Altekar, W.2
  • 39
    • 0024150562 scopus 로고
    • Alternative routes of carbohydrate metabolism in halophilic archaebacteria
    • Rawal, N.; Kelkar, S. M.; Altekar, W. Alternative routes of carbohydrate metabolism in halophilic archaebacteria Indian J. Biochem. Biophys. 1988, 25 (6) 674-86
    • (1988) Indian J. Biochem. Biophys. , vol.25 , Issue.6 , pp. 674-86
    • Rawal, N.1    Kelkar, S.M.2    Altekar, W.3
  • 40
    • 0035106495 scopus 로고    scopus 로고
    • Different glycolytic pathways for glucose and fructose in the halophilic archaeon Halococcus saccharolyticus
    • DOI 10.1007/s002030000237
    • Johnsen, U.; Selig, M.; Xavier, K. B.; Santos, H.; Schonheit, P. Different glycolytic pathways for glucose and fructose in the halophilic archaeon Halococcus saccharolyticus Arch. Microbiol. 2001, 175 (1) 52-61 (Pubitemid 32202030)
    • (2001) Archives of Microbiology , vol.175 , Issue.1 , pp. 52-61
    • Johnsen, U.1    Selig, M.2    Xavier, K.B.3    Santos, H.4    Schonheit, P.5
  • 41
    • 4444329994 scopus 로고    scopus 로고
    • Novel xylose dehydrogenase in the halophilic archaeon Haloarcula marismortui
    • DOI 10.1128/JB.186.18.6198-6207.2004
    • Johnsen, U.; Schonheit, P. Novel xylose dehydrogenase in the halophilic archaeon Haloarcula marismortui J. Bacteriol. 2004, 186 (18) 6198-207 (Pubitemid 39193289)
    • (2004) Journal of Bacteriology , vol.186 , Issue.18 , pp. 6198-6207
    • Johnsen, U.1    Schonheit, P.2
  • 43
    • 0024346543 scopus 로고
    • Structure and biosynthesis of prokaryotic glycoproteins
    • Lechner, J.; Wieland, F. Structure and biosynthesis of prokaryotic glycoproteins Annu. Rev. Biochem. 1989, 58, 173-94 (Pubitemid 19172968)
    • (1989) Annual Review of Biochemistry , vol.58 , pp. 173-194
    • Lechner, J.1    Wieland, F.2
  • 44
    • 0025572768 scopus 로고
    • Extracellular Ca2(+)-dependent inducible alkaline phosphatase from extremely halophilic archaebacterium Haloarcula marismortui
    • Goldman, S.; Hecht, K.; Eisenberg, H.; Mevarech, M. Extracellular Ca2(+)-dependent inducible alkaline phosphatase from extremely halophilic archaebacterium Haloarcula marismortui J. Bacteriol. 1990, 172 (12) 7065-70
    • (1990) J. Bacteriol. , vol.172 , Issue.12 , pp. 7065-70
    • Goldman, S.1    Hecht, K.2    Eisenberg, H.3    Mevarech, M.4
  • 45
    • 0022337274 scopus 로고
    • Halobacterial flagellins are sulfated glycoproteins
    • Wieland, F.; Paul, G.; Sumper, M. Halobacterial flagellins are sulfated glycoproteins J. Biol. Chem. 1985, 260 (28) 15180-5 (Pubitemid 16148009)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.28 , pp. 15180-15185
    • Wieland, F.1    Paul, G.2    Sumper, M.3
  • 47
    • 67650818533 scopus 로고    scopus 로고
    • A single transcription factor regulates evolutionarily diverse but functionally linked metabolic pathways in response to nutrient availability
    • Schmid, A. K.; Reiss, D. J.; Pan, M.; Koide, T.; Baliga, N. S. A single transcription factor regulates evolutionarily diverse but functionally linked metabolic pathways in response to nutrient availability Mol. Syst. Biol. 2009, 5, 282
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 282
    • Schmid, A.K.1    Reiss, D.J.2    Pan, M.3    Koide, T.4    Baliga, N.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.