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Volumn 327, Issue 2, 2003, Pages 347-357

Unique amino acid composition of proteins in halophilic bacteria

Author keywords

Amino acid composition; Genome comparison; Halophiles; Nucleotide composition; Protein surface

Indexed keywords

AMINO ACID; ASPARTIC ACID; BACTERIAL DNA; CYSTEINE; GLYCINE;

EID: 0037459217     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00150-5     Document Type: Article
Times cited : (221)

References (43)
  • 1
    • 0026646179 scopus 로고
    • Biochemical, structural, and molecular genetic aspects of halophilism
    • Eisenberg H., Mevarech M., Zaccai G. Biochemical, structural, and molecular genetic aspects of halophilism. Advan. Protein Chem. 43:1992;1-62.
    • (1992) Advan. Protein Chem. , vol.43 , pp. 1-62
    • Eisenberg, H.1    Mevarech, M.2    Zaccai, G.3
  • 2
    • 0026501434 scopus 로고
    • Solution studies of the elongation factor Tu from the extreme halophile Halobacterium marismortui
    • Ebel C., Guinet F., Langowski J., Urbanke C., Gagnon J., Zaccai G. Solution studies of the elongation factor Tu from the extreme halophile Halobacterium marismortui. J. Mol. Chem. 223:1992;361-371.
    • (1992) J. Mol. Chem. , vol.223 , pp. 361-371
    • Ebel, C.1    Guinet, F.2    Langowski, J.3    Urbanke, C.4    Gagnon, J.5    Zaccai, G.6
  • 3
    • 0028034679 scopus 로고
    • Stability against denaturation mechanisms in halophilic malate dehydrogenase "adapt" to solvent conditions
    • Bonnete F., Madern D., Zaccai G. Stability against denaturation mechanisms in halophilic malate dehydrogenase "adapt" to solvent conditions. J. Mol. Biol. 224:1994;436-447.
    • (1994) J. Mol. Biol. , vol.224 , pp. 436-447
    • Bonnete, F.1    Madern, D.2    Zaccai, G.3
  • 4
    • 0028953220 scopus 로고
    • Solution structure of glyceraldehyde-3-phosphate dehydrogenase from Haloarcula vallismortis
    • Ebel C., Altekar W., Langowski J., Urbanke C., Forest E., Zaccai G. Solution structure of glyceraldehyde-3-phosphate dehydrogenase from Haloarcula vallismortis. Biophys. Chem. 54:1995;219-227.
    • (1995) Biophys. Chem. , vol.54 , pp. 219-227
    • Ebel, C.1    Altekar, W.2    Langowski, J.3    Urbanke, C.4    Forest, E.5    Zaccai, G.6
  • 5
    • 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. 38:1974;272-290.
    • (1974) Bacteriol. Rev. , vol.38 , pp. 272-290
    • Lanyi, J.K.1
  • 6
    • 0019877658 scopus 로고
    • Structural stability of halophilic proteins
    • Rao J.K.M., Argos P. Structural stability of halophilic proteins. Biochemistry. 20:1981;6536-6543.
    • (1981) Biochemistry , vol.20 , pp. 6536-6543
    • Rao, J.K.M.1    Argos, P.2
  • 7
    • 0025101811 scopus 로고
    • Functional implications related to the gene structure of the elongation factor EF-Tu from Halobacterium marismortui
    • Baldacci G., Guinet F., Tillit J., Zaccai G., De Recondo A.M. Functional implications related to the gene structure of the elongation factor EF-Tu from Halobacterium marismortui. Nucl. Acids Res. 18:1990;507-511.
    • (1990) Nucl. Acids Res. , vol.18 , pp. 507-511
    • Baldacci, G.1    Guinet, F.2    Tillit, J.3    Zaccai, G.4    De Recondo, A.M.5
  • 8
    • 0025790495 scopus 로고
    • The genes for a halophilic glutamate dehydrogenase: Sequence, transcription analysis and phylogenetic implications
    • Benachenhou N., Baldacci G. The genes for a halophilic glutamate dehydrogenase: sequence, transcription analysis and phylogenetic implications. Mol. Gen. Genet. 230:1991;345-352.
    • (1991) Mol. Gen. Genet. , vol.230 , pp. 345-352
    • Benachenhou, N.1    Baldacci, G.2
  • 9
    • 0029027430 scopus 로고
    • Mutation at single acidic amino acid enhances the halophilic behaviour of malate dehydrogenase from Haloarcula marismortui in physiological salts
    • Madern D., Pfister C., Zaccai G. Mutation at single acidic amino acid enhances the halophilic behaviour of malate dehydrogenase from Haloarcula marismortui in physiological salts. Eur. J. Biochem. 230:1995;1088-1095.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 1088-1095
    • Madern, D.1    Pfister, C.2    Zaccai, G.3
  • 11
    • 37049069515 scopus 로고
    • A biophysical structure and solvent interactions in native and recombinant enzyme
    • Bonnete F., Madern D., Zaccai G. A biophysical structure and solvent interactions in native and recombinant enzyme. J. Chem. Soc., Faraday Trans. 89:1993;2659-2666.
    • (1993) J. Chem. Soc., Faraday Trans. , vol.89 , pp. 2659-2666
    • Bonnete, F.1    Madern, D.2    Zaccai, G.3
  • 12
    • 0030010138 scopus 로고    scopus 로고
    • Insights into protein adaptation to a saturated salt environment from the crystal structure of a halophilic 2Fe-2S ferredoxin
    • Frolow F., Harel M., Sussman J.L., Mevarech M., Shoham M. Insights into protein adaptation to a saturated salt environment from the crystal structure of a halophilic 2Fe-2S ferredoxin. Nature Struct. Biol. 3:1996;452-458.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 452-458
    • Frolow, F.1    Harel, M.2    Sussman, J.L.3    Mevarech, M.4    Shoham, M.5
  • 13
    • 0028014604 scopus 로고
    • Relevance of sequence statistics for the properties of extremophilic proteins
    • Bohm G., Jaenicke R. Relevance of sequence statistics for the properties of extremophilic proteins. Int. J. Peptide Protein Res. 43:1994;97-106.
    • (1994) Int. J. Peptide Protein Res. , vol.43 , pp. 97-106
    • Bohm, G.1    Jaenicke, R.2
  • 14
    • 0028084481 scopus 로고
    • A structure-based model for the halophilic adaptation dihydrofolate reductase from Haloferax volcanii
    • Bohm G., Jaenicke R. A structure-based model for the halophilic adaptation dihydrofolate reductase from Haloferax volcanii. Protein Eng. 7:1994;213-220.
    • (1994) Protein Eng. , vol.7 , pp. 213-220
    • Bohm, G.1    Jaenicke, R.2
  • 15
    • 0032563113 scopus 로고    scopus 로고
    • Electrostatic contributions to the stability of Halophilic proteins
    • Elock A.G., McCammon J.A. Electrostatic contributions to the stability of Halophilic proteins. J. Mol. Biol. 280:1998;731-748.
    • (1998) J. Mol. Biol. , vol.280 , pp. 731-748
    • Elock, A.G.1    McCammon, J.A.2
  • 17
    • 0035876479 scopus 로고    scopus 로고
    • Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria
    • Fukuchi S., Nishikawa K. Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria. J. Mol. Biol. 309:2001;835-843.
    • (2001) J. Mol. Biol. , vol.309 , pp. 835-843
    • Fukuchi, S.1    Nishikawa, K.2
  • 18
    • 0034767491 scopus 로고    scopus 로고
    • Understanding the adaptation of Halobacterium species NRC-1 to its extreme environment through computational analysis of its genome sequence
    • 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. 11:2001;1641-1650.
    • (2001) Genome Res. , vol.11 , pp. 1641-1650
    • Kennedy, S.P.1    Ng, W.V.2    Salzberg, S.L.3    Hood, L.4    DasSarma, S.5
  • 19
    • 0000800911 scopus 로고
    • Hydration of macromolecules. III. Hydration of polypeptides
    • Kuntz I.D. Hydration of macromolecules. III. Hydration of polypeptides. J. Am. Chem. Soc. 93:1971;514-516.
    • (1971) J. Am. Chem. Soc. , vol.93 , pp. 514-516
    • Kuntz, I.D.1
  • 20
    • 0031731672 scopus 로고    scopus 로고
    • Proteins from thermophilic and mesophilic organisms essentially do not differ in packing
    • Karshikoff A., Ladenstein R. Proteins from thermophilic and mesophilic organisms essentially do not differ in packing. Protein Eng. 11:1998;867-872.
    • (1998) Protein Eng. , vol.11 , pp. 867-872
    • Karshikoff, A.1    Ladenstein, R.2
  • 22
    • 0033554840 scopus 로고    scopus 로고
    • Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface
    • Loladze V.V., Molero-Ibarra B., Sanchez-Ruiz J.M., Makhatadze G.I. Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface. Biochemistry. 38:1999;16419-16423.
    • (1999) Biochemistry , vol.38 , pp. 16419-16423
    • Loladze, V.V.1    Molero-Ibarra, B.2    Sanchez-Ruiz, J.M.3    Makhatadze, G.I.4
  • 23
    • 0034620528 scopus 로고    scopus 로고
    • Rational modification of protein stability by the mutation of charged surface residues
    • Spector S., Wang M., Carp S.A., Robblee J., Hendsch Z.S., Fairman R., et al. Rational modification of protein stability by the mutation of charged surface residues. Biochemistry. 39:2000;872-879.
    • (2000) Biochemistry , vol.39 , pp. 872-879
    • Spector, S.1    Wang, M.2    Carp, S.A.3    Robblee, J.4    Hendsch, Z.S.5    Fairman, R.6
  • 24
    • 0034100848 scopus 로고    scopus 로고
    • Two exposed amino acid residues confer thermostability on a cold shock protein
    • Perl D., Mueller U., Heinemann U., Schmid F.X. Two exposed amino acid residues confer thermostability on a cold shock protein. Nature Struct. Biol. 7:2000;380-383.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 380-383
    • Perl, D.1    Mueller, U.2    Heinemann, U.3    Schmid, F.X.4
  • 25
    • 0032582395 scopus 로고    scopus 로고
    • Genes from nine genomes are separated into their organisms in the dinucleotide composition space
    • Nakashima H., Ota M., Nishikawa K., Ooi T. Genes from nine genomes are separated into their organisms in the dinucleotide composition space. DNA Res. 5:1998;251-259.
    • (1998) DNA Res. , vol.5 , pp. 251-259
    • Nakashima, H.1    Ota, M.2    Nishikawa, K.3    Ooi, T.4
  • 26
    • 0029060923 scopus 로고
    • Dinucleotide relative abundance extremes: A genomic signature
    • Karlin S., Burge C. Dinucleotide relative abundance extremes: a genomic signature. Trends Genet. 11:1995;238-290.
    • (1995) Trends Genet. , vol.11 , pp. 238-290
    • Karlin, S.1    Burge, C.2
  • 27
    • 0033102134 scopus 로고    scopus 로고
    • Overexpression of salt-tolerant glutaminase from Micrococcus luteus K-3 in Escherichia coli and its purification
    • Nandakumar R., Wakayama M., Nagano Y., Kawamura T., Sakai K., Moriguchi M. Overexpression of salt-tolerant glutaminase from Micrococcus luteus K-3 in Escherichia coli and its purification. Protein Expr. Purif. 15:1999;155-161.
    • (1999) Protein Expr. Purif. , vol.15 , pp. 155-161
    • Nandakumar, R.1    Wakayama, M.2    Nagano, Y.3    Kawamura, T.4    Sakai, K.5    Moriguchi, M.6
  • 29
    • 0033609333 scopus 로고    scopus 로고
    • Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritime
    • Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., et al. Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritime. Nature. 399:1999;323-329.
    • (1999) Nature , vol.399 , pp. 323-329
    • Nelson, K.E.1    Clayton, R.A.2    Gill, S.R.3    Gwinn, M.L.4    Dodson, R.J.5    Haft, D.H.6
  • 30
    • 0033616977 scopus 로고    scopus 로고
    • Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1
    • Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., et al. Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1. DNA Res. 6:1999;83-101.
    • (1999) DNA Res. , vol.6 , pp. 83-101
    • Kawarabayasi, Y.1    Hino, Y.2    Horikawa, H.3    Yamazaki, S.4    Haikawa, Y.5    Jin-No, K.6
  • 31
    • 15644383855 scopus 로고    scopus 로고
    • Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: Functional analysis and comparative genomics
    • Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H., Dubois J., Aldredge T., et al. Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics. J. Bacteriol. 179:1997;7135-7155.
    • (1997) J. Bacteriol. , vol.179 , pp. 7135-7155
    • Smith, D.R.1    Doucette-Stamm, L.A.2    Deloughery, C.3    Lee, H.4    Dubois, J.5    Aldredge, T.6
  • 35
    • 0030731108 scopus 로고    scopus 로고
    • The complete genome sequence of the Gram-positive bacterium Bacillus subtilis
    • Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., et al. The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. Nature. 390:1997;249-256.
    • (1997) Nature , vol.390 , pp. 249-256
    • Kunst, F.1    Ogasawara, N.2    Moszer, I.3    Albertini, A.M.4    Alloni, G.5    Azevedo, V.6
  • 36
    • 0032893084 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1999
    • Bairoch A., Apweiler R. The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1999. Nucl. Acids Res. 27:1999;49-54.
    • (1999) Nucl. Acids Res. , vol.27 , pp. 49-54
    • Bairoch, A.1    Apweiler, R.2
  • 39
    • 0028239038 scopus 로고
    • Discrimination of intracellular and extracellular proteins using amino acid composition and residue-pair frequencies
    • Nakashima H., Nishikawa K. Discrimination of intracellular and extracellular proteins using amino acid composition and residue-pair frequencies. J. Mol. Biol. 238:1994;54-61.
    • (1994) J. Mol. Biol. , vol.238 , pp. 54-61
    • Nakashima, H.1    Nishikawa, K.2
  • 40
    • 0031826040 scopus 로고    scopus 로고
    • SOSUI:classification and secondary structure prediction system for membrane proteins
    • Hirokawa T., Boon-Chieng S., Mitaku S. SOSUI:classification and secondary structure prediction system for membrane proteins. Bioinformatics. 14:1998;378-379.
    • (1998) Bioinformatics , vol.14 , pp. 378-379
    • Hirokawa, T.1    Boon-Chieng, S.2    Mitaku, S.3
  • 41
    • 0033044637 scopus 로고    scopus 로고
    • Machine learning approaches to the prediction of signal peptides and other protein sorting signals
    • Nielsen H., Brunak S., von Heijne G. Machine learning approaches to the prediction of signal peptides and other protein sorting signals. Protein Eng. 12:1999;3-9.
    • (1999) Protein Eng. , vol.12 , pp. 3-9
    • Nielsen, H.1    Brunak, S.2    Von Heijne, G.3
  • 42
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymer. 22:1983;2577-2637.
    • (1983) Biopolymer , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 43
    • 0017588168 scopus 로고
    • A study of the preferred environment of amino acid residues in globular proteins
    • Manavalan P., Ponnuswamy P.K. A study of the preferred environment of amino acid residues in globular proteins. Arch. Biochem. Biophys. 184:1977;476-487.
    • (1977) Arch. Biochem. Biophys. , vol.184 , pp. 476-487
    • Manavalan, P.1    Ponnuswamy, P.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.