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Volumn 529, Issue 7586, 2016, Pages 358-363

Codon influence on protein expression in E. coli correlates with mRNA levels

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BACTERIAL RNA; MESSENGER RNA; BACTERIOPHAGE T7 RNA POLYMERASE; CODON; DNA DIRECTED RNA POLYMERASE; ESCHERICHIA COLI PROTEIN; SYNTHETIC DNA; VIRAL PROTEIN;

EID: 84955442598     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature16509     Document Type: Article
Times cited : (306)

References (62)
  • 1
    • 0027960812 scopus 로고
    • Role of the AGA/AGG codons, the rarest codons in global gene expression in Escherichia coli
    • Chen, G. T. & Inouye, M. Role of the AGA/AGG codons, the rarest codons in global gene expression in Escherichia coli. Genes Dev. 8, 2641-2652 (1994).
    • (1994) Genes Dev. , vol.8 , pp. 2641-2652
    • Chen, G.T.1    Inouye, M.2
  • 2
    • 0029924182 scopus 로고    scopus 로고
    • Synonymous codon selection controls in vivo turnover and amount of mRNA in Escherichia coli bla and ompA genes
    • Deana, A., Ehrlich, R. & Reiss, C. Synonymous codon selection controls in vivo turnover and amount of mRNA in Escherichia coli bla and ompA genes. J. Bacteriol. 178, 2718-2720 (1996).
    • (1996) J. Bacteriol. , vol.178 , pp. 2718-2720
    • Deana, A.1    Ehrlich, R.2    Reiss, C.3
  • 3
    • 64849114915 scopus 로고    scopus 로고
    • Coding-sequence determinants of gene expression in Escherichia coli
    • Kudla, G., Murray, A. W., Tollervey, D. & Plotkin, J. B. Coding-sequence determinants of gene expression in Escherichia coli. Science 324, 255-258 (2009).
    • (2009) Science , vol.324 , pp. 255-258
    • Kudla, G.1    Murray, A.W.2    Tollervey, D.3    Plotkin, J.B.4
  • 4
    • 77649245858 scopus 로고    scopus 로고
    • Translation efficiency is determined by both codon bias and folding energy
    • Tuller, T., Waldman, Y. Y., Kupiec, M. & Ruppin, E. Translation efficiency is determined by both codon bias and folding energy. Proc. Natl Acad. Sci. USA 107, 3645-3650 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 3645-3650
    • Tuller, T.1    Waldman, Y.Y.2    Kupiec, M.3    Ruppin, E.4
  • 5
    • 84886302057 scopus 로고    scopus 로고
    • Causes and effects of N-terminal codon bias in bacterial genes
    • Goodman, D. B., Church, G. M. & Kosuri, S. Causes and effects of N-terminal codon bias in bacterial genes. Science 342, 475-479 (2013).
    • (2013) Science , vol.342 , pp. 475-479
    • Goodman, D.B.1    Church, G.M.2    Kosuri, S.3
  • 6
    • 84857045212 scopus 로고    scopus 로고
    • Adenine-containing codons enhance protein synthesis by promoting mRNA binding to ribosomal 30S subunits provided that specific tRNAs are not exhausted
    • Castillo-Méndez, M. A., Jacinto-Loeza, E., Olivares-Trejo, J. J., Guarneros-Pena, G. & Hernandez-Sanchez, J. Adenine-containing codons enhance protein synthesis by promoting mRNA binding to ribosomal 30S subunits provided that specific tRNAs are not exhausted. Biochimie 94, 662-672 (2012).
    • (2012) Biochimie , vol.94 , pp. 662-672
    • Castillo-Méndez, M.A.1    Jacinto-Loeza, E.2    Olivares-Trejo, J.J.3    Guarneros-Pena, G.4    Hernandez-Sanchez, J.5
  • 9
    • 84865098071 scopus 로고    scopus 로고
    • Silent substitutions predictably alter translation elongation rates and protein folding efficiencies
    • Spencer, P. S., Siller, E., Anderson, J. F. & Barral, J. M. Silent substitutions predictably alter translation elongation rates and protein folding efficiencies. J. Mol. Biol. 422, 328-335 (2012).
    • (2012) J. Mol. Biol. , vol.422 , pp. 328-335
    • Spencer, P.S.1    Siller, E.2    Anderson, J.F.3    Barral, J.M.4
  • 10
    • 84899550455 scopus 로고    scopus 로고
    • Quantifying absolute protein synthesis rates reveals principles underlying allocation of cellular resources
    • Li, G. W., Burkhardt, D., Gross, C. & Weissman, J. S. Quantifying absolute protein synthesis rates reveals principles underlying allocation of cellular resources. Cell 157, 624-635 (2014).
    • (2014) Cell , vol.157 , pp. 624-635
    • Li, G.W.1    Burkhardt, D.2    Gross, C.3    Weissman, J.S.4
  • 11
    • 84860231100 scopus 로고    scopus 로고
    • The anti-Shine-Dalgarno sequence drives translational pausing and codon choice in bacteria
    • Li, G.-W., Oh, E. & Weissman, J. S. The anti-Shine-Dalgarno sequence drives translational pausing and codon choice in bacteria. Nature 484, 538-541 (2012).
    • (2012) Nature , vol.484 , pp. 538-541
    • Li, G.-W.1    Oh, E.2    Weissman, J.S.3
  • 12
    • 79954456859 scopus 로고    scopus 로고
    • Determinants of translation efficiency and accuracy
    • Gingold, H. & Pilpel, Y. Determinants of translation efficiency and accuracy. Mol. Syst. Biol. 7, 481 (2011).
    • (2011) Mol. Syst. Biol. , vol.7 , pp. 481
    • Gingold, H.1    Pilpel, Y.2
  • 13
    • 77951734603 scopus 로고    scopus 로고
    • A role for codon order in translation dynamics
    • Cannarozzi, G. et al. A role for codon order in translation dynamics. Cell 141, 355-367 (2010).
    • (2010) Cell , vol.141 , pp. 355-367
    • Cannarozzi, G.1
  • 14
    • 0023650543 scopus 로고
    • The codon adaptation index-A measure of directional synonymous codon usage bias, and its potential applications
    • Sharp, P. M. & Li, W. H. The codon adaptation index-a measure of directional synonymous codon usage bias, and its potential applications. Nucleic Acids Res. 15, 1281-1295 (1987).
    • (1987) Nucleic Acids Res. , vol.15 , pp. 1281-1295
    • Sharp, P.M.1    Li, W.H.2
  • 15
    • 0022554039 scopus 로고
    • Fine tuning of ribosomal accuracy
    • Ninio, J. Fine tuning of ribosomal accuracy. FEBS Lett. 196, 1-4 (1986).
    • (1986) FEBS Lett. , vol.196 , pp. 1-4
    • Ninio, J.1
  • 16
    • 77951715627 scopus 로고    scopus 로고
    • An evolutionarily conserved mechanism for controlling the efficiency of protein translation
    • Tuller, T. et al. An evolutionarily conserved mechanism for controlling the efficiency of protein translation. Cell 141, 344-354 (2010).
    • (2010) Cell , vol.141 , pp. 344-354
    • Tuller, T.1
  • 17
    • 84877767258 scopus 로고    scopus 로고
    • Estimating selection on synonymous codon usage from noisy experimental data
    • Wallace, E. W., Airoldi, E. M. & Drummond, D. A. Estimating selection on synonymous codon usage from noisy experimental data. Mol. Biol. Evol. 30, 1438-1453 (2013).
    • (2013) Mol. Biol. Evol. , vol.30 , pp. 1438-1453
    • Wallace, E.W.1    Airoldi, E.M.2    Drummond, D.A.3
  • 18
    • 0014414244 scopus 로고
    • RNA codons and protein synthesis. 15. Dissimilar responses of mammalian and bacterial transfer RNA fractions to messenger RNA codons
    • Caskey, C. T., Beaudet, A. & Nirenberg, M. RNA codons and protein synthesis. 15. Dissimilar responses of mammalian and bacterial transfer RNA fractions to messenger RNA codons. J. Mol. Biol. 37, 99-118 (1968).
    • (1968) J. Mol. Biol. , vol.37 , pp. 99-118
    • Caskey, C.T.1    Beaudet, A.2    Nirenberg, M.3
  • 19
    • 0019824131 scopus 로고
    • Correlation between the abundance of Escherichia coli transfer RNAs and the occurrence of the respective codons in its protein genes: A proposal for a synonymous codon choice that is optimal for the E. Coli translational system
    • Ikemura, T. Correlation between the abundance of Escherichia coli transfer RNAs and the occurrence of the respective codons in its protein genes: a proposal for a synonymous codon choice that is optimal for the E. coli translational system. J. Mol. Biol. 151, 389-409 (1981).
    • (1981) J. Mol. Biol. , vol.151 , pp. 389-409
    • Ikemura, T.1
  • 20
    • 0023734317 scopus 로고
    • Codon and amino-acid specificities of a transfer RNA are both converted by a single post-transcriptional modification
    • Muramatsu, T. et al. Codon and amino-acid specificities of a transfer RNA are both converted by a single post-transcriptional modification. Nature 336, 179-181 (1988).
    • (1988) Nature , vol.336 , pp. 179-181
    • Muramatsu, T.1
  • 21
    • 0026010217 scopus 로고
    • Low-usage codons in Escherichia coli, yeast, fruit fly and primates
    • Zhang, S. P., Zubay, G. & Goldman, E. Low-usage codons in Escherichia coli, yeast, fruit fly and primates. Gene 105, 61-72 (1991).
    • (1991) Gene , vol.105 , pp. 61-72
    • Zhang, S.P.1    Zubay, G.2    Goldman, E.3
  • 22
    • 0025941139 scopus 로고
    • The selection-mutation-drift theory of synonymous codon usage
    • Bulmer, M. The selection-mutation-drift theory of synonymous codon usage. Genetics 129, 897-907 (1991).
    • (1991) Genetics , vol.129 , pp. 897-907
    • Bulmer, M.1
  • 23
    • 0030564828 scopus 로고    scopus 로고
    • Co-variation of tRNA abundance and codon usage in Escherichia coli at different growth rates
    • Dong, H., Nilsson, L. & Kurland, C. G. Co-variation of tRNA abundance and codon usage in Escherichia coli at different growth rates. J. Mol. Biol. 260, 649-663 (1996).
    • (1996) J. Mol. Biol. , vol.260 , pp. 649-663
    • Dong, H.1    Nilsson, L.2    Kurland, C.G.3
  • 24
    • 0038179369 scopus 로고    scopus 로고
    • Selective charging of tRNA isoacceptors explains patterns of codon usage
    • Elf, J., Nilsson, D., Tenson, T. & Ehrenberg, M. Selective charging of tRNA isoacceptors explains patterns of codon usage. Science 300, 1718-1722 (2003).
    • (2003) Science , vol.300 , pp. 1718-1722
    • Elf, J.1    Nilsson, D.2    Tenson, T.3    Ehrenberg, M.4
  • 25
    • 14644396660 scopus 로고    scopus 로고
    • Selective charging of tRNA isoacceptors induced by amino-acid starvation
    • Dittmar, K. A., Sorensen, M. A., Elf, J., Ehrenberg, M. & Pan, T. Selective charging of tRNA isoacceptors induced by amino-acid starvation. EMBO Rep. 6, 151-157 (2005).
    • (2005) EMBO Rep. , vol.6 , pp. 151-157
    • Dittmar, K.A.1    Sorensen, M.A.2    Elf, J.3    Ehrenberg, M.4    Pan, T.5
  • 26
    • 77956663124 scopus 로고    scopus 로고
    • Differential arginylation of actin isoforms is regulated by coding sequence-dependent degradation
    • Zhang, F., Saha, S., Shabalina, S. A. & Kashina, A. Differential arginylation of actin isoforms is regulated by coding sequence-dependent degradation. Science 329, 1534-1537 (2010).
    • (2010) Science , vol.329 , pp. 1534-1537
    • Zhang, F.1    Saha, S.2    Shabalina, S.A.3    Kashina, A.4
  • 27
    • 84858298050 scopus 로고    scopus 로고
    • Protein synthesis factors (RF1, RF2, RF3, RRF, and tmRNA) and peptidyl-tRNA hydrolase rescue stalled ribosomes at sense codons
    • Vivanco-Domínguez, S. et al. Protein synthesis factors (RF1, RF2, RF3, RRF, and tmRNA) and peptidyl-tRNA hydrolase rescue stalled ribosomes at sense codons. J. Mol. Biol. 417, 425-439 (2012).
    • (2012) J. Mol. Biol. , vol.417 , pp. 425-439
    • Vivanco-Domínguez, S.1
  • 28
    • 84906235471 scopus 로고    scopus 로고
    • The effect of tRNA levels on decoding times of mRNA codons
    • Dana, A. & Tuller, T. The effect of tRNA levels on decoding times of mRNA codons. Nucleic Acids Res. 42, 9171-9181 (2014).
    • (2014) Nucleic Acids Res. , vol.42 , pp. 9171-9181
    • Dana, A.1    Tuller, T.2
  • 29
    • 84930682682 scopus 로고    scopus 로고
    • Widespread co-translational RNA decay reveals ribosome dynamics
    • Pelechano, V. & Wei, W. & Steinmetz, Lars M. Widespread co-translational RNA decay reveals ribosome dynamics. Cell 161, 1400-1412 (2015).
    • (2015) Cell , vol.161 , pp. 1400-1412
    • Pelechano, V.1    Wei, W.2    Steinmetz, L.M.3
  • 30
    • 84924567669 scopus 로고    scopus 로고
    • Codon optimality is a major determinant of mRNA stability
    • Presnyak, V. et al. Codon optimality is a major determinant of mRNA stability. Cell 160, 1111-1124 (2015).
    • (2015) Cell , vol.160 , pp. 1111-1124
    • Presnyak, V.1
  • 31
    • 47549097539 scopus 로고    scopus 로고
    • Mistranslation-induced protein misfolding as a dominant constraint on coding-sequence evolution
    • Drummond, D. A. & Wilke, C. O. Mistranslation-induced protein misfolding as a dominant constraint on coding-sequence evolution. Cell 134, 341-352 (2008).
    • (2008) Cell , vol.134 , pp. 341-352
    • Drummond, D.A.1    Wilke, C.O.2
  • 32
    • 0024300837 scopus 로고
    • Influence of duplexes 3′ to the mRNA initiation codon on the efficiency of monosome formation
    • Shakin-Eshleman, S. H. & Liebhaber, S. A. Influence of duplexes 3′ to the mRNA initiation codon on the efficiency of monosome formation. Biochemistry 27, 3975-3982 (1988).
    • (1988) Biochemistry , vol.27 , pp. 3975-3982
    • Shakin-Eshleman, S.H.1    Liebhaber, S.A.2
  • 33
    • 84884141974 scopus 로고    scopus 로고
    • Differential translation tunes uneven production of operonencoded proteins
    • Quax, T. E. et al. Differential translation tunes uneven production of operonencoded proteins. Cell Rep. 4, 938-944 (2013).
    • (2013) Cell Rep. , vol.4 , pp. 938-944
    • Quax, T.E.1
  • 34
    • 84883142045 scopus 로고    scopus 로고
    • Translation of CGA codon repeats in yeast involves quality control components and ribosomal protein L1
    • Letzring, D. P., Wolf, A. S., Brule, C. E. & Grayhack, E. J. Translation of CGA codon repeats in yeast involves quality control components and ribosomal protein L1. RNA 19, 1208-1217 (2013).
    • (2013) RNA , vol.19 , pp. 1208-1217
    • Letzring, D.P.1    Wolf, A.S.2    Brule, C.E.3    Grayhack, E.J.4
  • 35
    • 84871918588 scopus 로고    scopus 로고
    • Translation elongation factor EF-P alleviates ribosome stalling at polyproline stretches
    • Ude, S. et al. Translation elongation factor EF-P alleviates ribosome stalling at polyproline stretches. Science 339, 82-85 (2013).
    • (2013) Science , vol.339 , pp. 82-85
    • Ude, S.1
  • 36
    • 0029026714 scopus 로고
    • The stability of Escherichia coli lacZ mRNA depends upon the simultaneity of its synthesis and translation
    • Iost, I. & Dreyfus, M. The stability of Escherichia coli lacZ mRNA depends upon the simultaneity of its synthesis and translation. EMBO J. 14, 3252-3261 (1995).
    • (1995) EMBO J. , vol.14 , pp. 3252-3261
    • Iost, I.1    Dreyfus, M.2
  • 37
    • 0026544038 scopus 로고
    • Bacteriophage T7 RNA polymerase travels far ahead of ribosomes in vivo
    • Iost, I., Guillerez, J. & Dreyfus, M. Bacteriophage T7 RNA polymerase travels far ahead of ribosomes in vivo. J. Bacteriol. 174, 619-622 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 619-622
    • Iost, I.1    Guillerez, J.2    Dreyfus, M.3
  • 38
    • 20144387833 scopus 로고    scopus 로고
    • Robotic cloning and protein production platform of the Northeast Structural Genomics Consortium
    • Acton, T. B. et al. Robotic cloning and protein production platform of the Northeast Structural Genomics Consortium. Methods Enzymol. 394, 210-243 (2005).
    • (2005) Methods Enzymol. , vol.394 , pp. 210-243
    • Acton, T.B.1
  • 39
    • 84887410233 scopus 로고    scopus 로고
    • Large-scale experimental studies show unexpected amino acid effects on protein expression and solubility in vivo in E. Coli
    • Price, W. N. et al. Large-scale experimental studies show unexpected amino acid effects on protein expression and solubility in vivo in E. coli. Microb. Inform. Exp. 1, 6 (2011).
    • (2011) Microb. Inform. Exp. , vol.1 , pp. 6
    • Price, W.N.1
  • 40
    • 84892773271 scopus 로고    scopus 로고
    • Escherichia coli ribosomal protein S1 unfolds structured mRNAs onto the ribosome for active translation initiation
    • Duval, M. et al. Escherichia coli ribosomal protein S1 unfolds structured mRNAs onto the ribosome for active translation initiation. PLoS Biol. 11, e1001731 (2013).
    • (2013) PLoS Biol. , vol.11 , pp. e1001731
    • Duval, M.1
  • 41
    • 77949447172 scopus 로고    scopus 로고
    • RNAstructure: Software for RNA secondary structure prediction and analysis
    • Reuter, J. S. & Mathews, D. H. RNAstructure: software for RNA secondary structure prediction and analysis. BMC Bioinformatics 11, 129 (2010).
    • (2010) BMC Bioinformatics , vol.11 , pp. 129
    • Reuter, J.S.1    Mathews, D.H.2
  • 42
    • 54249096045 scopus 로고    scopus 로고
    • Electrostatics in the ribosomal tunnel modulate chain elongation rates
    • Lu, J. & Deutsch, C. Electrostatics in the ribosomal tunnel modulate chain elongation rates. J. Mol. Biol. 384, 73-86 (2008).
    • (2008) J. Mol. Biol. , vol.384 , pp. 73-86
    • Lu, J.1    Deutsch, C.2
  • 43
    • 42049108914 scopus 로고    scopus 로고
    • Protein abundance profiling of the Escherichia coli cytosol
    • Ishihama, Y. et al. Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9, 102 (2008).
    • (2008) BMC Genomics , vol.9 , pp. 102
    • Ishihama, Y.1
  • 44
    • 84922888717 scopus 로고    scopus 로고
    • Genome-wide study of mRNA degradation and transcript elongation in Escherichia coli
    • Chen, H., Shiroguchi, K., Ge, H. & Xie, X. S. Genome-wide study of mRNA degradation and transcript elongation in Escherichia coli. Mol. Syst. Biol. 11, 781 (2015).
    • (2015) Mol. Syst. Biol. , vol.11 , pp. 781
    • Chen, H.1    Shiroguchi, K.2    Ge, H.3    Xie, X.S.4
  • 45
    • 0344237338 scopus 로고    scopus 로고
    • Unexpected correlations between gene expression and codon usage bias from microarray data for the whole Escherichia coli K-12 genome
    • dos Reis, M. Unexpected correlations between gene expression and codon usage bias from microarray data for the whole Escherichia coli K-12 genome. Nucleic Acids Res. 31, 6976-6985 (2003).
    • (2003) Nucleic Acids Res. , vol.31 , pp. 6976-6985
    • Dos Reis, M.1
  • 46
    • 0035919778 scopus 로고    scopus 로고
    • The relationship between translational control and mRNA degradation for the Escherichia coli threonyltRNA synthetase gene
    • Nogueira, T., de Smit, M., Graffe, M. & Springer, M. The relationship between translational control and mRNA degradation for the Escherichia coli threonyltRNA synthetase gene. J. Mol. Biol. 310, 709-722 (2001).
    • (2001) J. Mol. Biol. , vol.310 , pp. 709-722
    • Nogueira, T.1    De Smit, M.2    Graffe, M.3    Springer, M.4
  • 48
    • 21744443970 scopus 로고    scopus 로고
    • TmRNA-induced release of messenger RNA from stalled ribosomes
    • Ivanova, N., Pavlov, M. Y. & Ehrenberg, M. tmRNA-induced release of messenger RNA from stalled ribosomes. J. Mol. Biol. 350, 897-905 (2005).
    • (2005) J. Mol. Biol. , vol.350 , pp. 897-905
    • Ivanova, N.1    Pavlov, M.Y.2    Ehrenberg, M.3
  • 49
    • 77957935294 scopus 로고    scopus 로고
    • Dom34:Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to initiate no-go decay
    • Shoemaker, C. J., Eyler, D. E. & Green, R. Dom34:Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to initiate no-go decay. Science 330, 369-372 (2010).
    • (2010) Science , vol.330 , pp. 369-372
    • Shoemaker, C.J.1    Eyler, D.E.2    Green, R.3
  • 50
    • 79955008757 scopus 로고    scopus 로고
    • Escherichia coli YaeJ protein mediates a novel ribosome-rescue pathway distinct from SsrA- and ArfA-mediated pathways
    • Chadani, Y., Ono, K., Kutsukake, K. & Abo, T. Escherichia coli YaeJ protein mediates a novel ribosome-rescue pathway distinct from SsrA- and ArfA-mediated pathways. Mol. Microbiol. 80, 772-785 (2011).
    • (2011) Mol. Microbiol. , vol.80 , pp. 772-785
    • Chadani, Y.1    Ono, K.2    Kutsukake, K.3    Abo, T.4
  • 51
    • 77956187416 scopus 로고    scopus 로고
    • The high-throughput protein sample production platform of the Northeast Structural Genomics Consortium
    • Xiao, R. et al. The high-throughput protein sample production platform of the Northeast Structural Genomics Consortium. J. Struct. Biol. 172, 21-33 (2010).
    • (2010) J. Struct. Biol. , vol.172 , pp. 21-33
    • Xiao, R.1
  • 52
    • 79952411326 scopus 로고    scopus 로고
    • Preparation of protein samples for NMR structure, function, and small-molecule screening studies
    • Acton, T. B. et al. Preparation of protein samples for NMR structure, function, and small-molecule screening studies. Methods Enzymol. 493, 21-60 (2011).
    • (2011) Methods Enzymol. , vol.493 , pp. 21-60
    • Acton, T.B.1
  • 54
    • 0016355478 scopus 로고
    • A new look at the statistical model identification
    • Akaike, H. A new look at the statistical model identification. IEEE Trans. Auto. Con. 19, 716-723 (1974).
    • (1974) IEEE Trans. Auto. Con. , vol.19 , pp. 716-723
    • Akaike, H.1
  • 56
    • 0030095165 scopus 로고    scopus 로고
    • 13C-enriched fusion proteins in Escherichia coli
    • 13C-enriched fusion proteins in Escherichia coli. J. Biomol. NMR 7, 131-141 (1996).
    • (1996) J. Biomol. NMR , vol.7 , pp. 131-141
    • Jansson, M.1
  • 57
    • 84876556918 scopus 로고    scopus 로고
    • EcoCyc: Fusing model organism databases with systems biology
    • Keseler, I. M. et al. EcoCyc: fusing model organism databases with systems biology. Nucleic Acids Res. 41, D605-D612 (2013).
    • (2013) Nucleic Acids Res. , vol.41 , pp. D605-D612
    • Keseler, I.M.1
  • 58
    • 0041341888 scopus 로고    scopus 로고
    • Prediction of lipoprotein signal peptides in Gram-negative bacteria
    • Juncker, A. S. et al. Prediction of lipoprotein signal peptides in Gram-negative bacteria. Protein Sci. 12, 1652-1662 (2003).
    • (2003) Protein Sci. , vol.12 , pp. 1652-1662
    • Juncker, A.S.1
  • 59
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • 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. 305, 567-580 (2001).
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 60
    • 0001389945 scopus 로고
    • Enzyme induction as an all-or-none phenomenon
    • Novick, A. & Weiner, M. Enzyme induction as an all-or-none phenomenon. Proc. Natl Acad. Sci. USA 43, 553-566 (1957).
    • (1957) Proc. Natl Acad. Sci. USA , vol.43 , pp. 553-566
    • Novick, A.1    Weiner, M.2
  • 61
    • 0027471964 scopus 로고
    • The use of lac-type promoters in control analysis
    • Jensen, P. R., Westerhoff, H. V. & Michelsen, O. The use of lac-type promoters in control analysis. Eur. J. Biochem. 211, 181-191 (1993).
    • (1993) Eur. J. Biochem. , vol.211 , pp. 181-191
    • Jensen, P.R.1    Westerhoff, H.V.2    Michelsen, O.3
  • 62
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L. M., Belin, D., Carson, M. J. & Beckwith, J. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177, 4121-4130 (1995).
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.