메뉴 건너뛰기




Volumn 18, Issue 3, 2000, Pages 394-403

Short, hydrophobic, alanine-based proteins based on the basic region/leucine zipper protein motif: Overcoming inclusion body formation and protein aggregation during overexpression, purification, and renaturation

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA HELIX; AMINO ACID SUBSTITUTION; BASIC REGION LEUCINE ZIPPER PROTEIN MOTIF; BINDING SITE; HYDROPHOBICITY; PROTEIN AGGREGATION; PROTEIN DENATURATION; PROTEIN DNA BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN RENATURATION; RENATURATION;

EID: 0034051459     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2000.1209     Document Type: Article
Times cited : (19)

References (27)
  • 1
    • 0022981167 scopus 로고
    • Saturation mutagenesis of the yeast his3 regulatory site: Requirements for transcriptional induction and for binding by GCN4 activator protein
    • Hill D. E., Hope I. A., Macke J. P., Struhl K. Saturation mutagenesis of the yeast his3 regulatory site: Requirements for transcriptional induction and for binding by GCN4 activator protein. Science. 234:1986;451-457
    • (1986) Science , vol.234 , pp. 451-457
    • Hill, D.E.1    Hope, I.A.2    Macke, J.P.3    Struhl, K.4
  • 2
    • 0027377202 scopus 로고
    • The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility
    • König P., Richmond T. J. The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility. J. Mol. Biol. 233:1993;139-154
    • (1993) J. Mol. Biol. , vol.233 , pp. 139-154
    • König, P.1    Richmond, T.J.2
  • 3
    • 0027049805 scopus 로고
    • The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted α helices: Crystal structure of the protein-DNA complex
    • Ellenberger T. E., Brandl C. J., Struhl K., Harrison S. C. The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted α helices: Crystal structure of the protein-DNA complex. Cell. 71:1992;1223-1237
    • (1992) Cell , vol.71 , pp. 1223-1237
    • Ellenberger, T.E.1    Brandl, C.J.2    Struhl, K.3    Harrison, S.C.4
  • 4
    • 0029563634 scopus 로고
    • Crystal structure of a bZIP/DNA complex at 2.2 Å: Determinants of DNA specific recognition
    • Keller W., König P., Richmond T. J. Crystal structure of a bZIP/DNA complex at 2.2 Å: Determinants of DNA specific recognition. J. Mol. Biol. 254:1995;657-667
    • (1995) J. Mol. Biol. , vol.254 , pp. 657-667
    • Keller, W.1    König, P.2    Richmond, T.J.3
  • 5
    • 0028894384 scopus 로고
    • Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA
    • Glover J. N. M., Harrison S. C. Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA. Nature. 373:1995;257-261
    • (1995) Nature , vol.373 , pp. 257-261
    • Glover, J.N.M.1    Harrison, S.C.2
  • 6
    • 0026682657 scopus 로고
    • Transcription factors: Structural families and principles of DNA recognition
    • Pabo C. O., Sauer R. T. Transcription factors: Structural families and principles of DNA recognition. Annu. Rev. Biochem. 61:1992;1053-1095
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 1053-1095
    • Pabo, C.O.1    Sauer, R.T.2
  • 7
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Neil K. T., DeGrado W. F. A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science. 250:1990;646-651
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 8
    • 0029958659 scopus 로고    scopus 로고
    • Structure-based thermodynamic scale of α-helix propensities in amino acids
    • Luque I., Mayorga O. L., Freire E. Structure-based thermodynamic scale of α-helix propensities in amino acids. Biochemistry. 35:1996;13681-13688
    • (1996) Biochemistry , vol.35 , pp. 13681-13688
    • Luque, I.1    Mayorga, O.L.2    Freire, E.3
  • 9
    • 0025991706 scopus 로고
    • DNA-induced increase in the α-helical content of C/EBP and GCN4
    • O'Neil K. T., Shuman J. D., Ampe C., DeGrado W. F. DNA-induced increase in the α-helical content of C/EBP and GCN4. Biochemistry. 30:1991;9030-9034
    • (1991) Biochemistry , vol.30 , pp. 9030-9034
    • O'Neil, K.T.1    Shuman, J.D.2    Ampe, C.3    DeGrado, W.F.4
  • 10
    • 0025865320 scopus 로고
    • Solution structure of the basic region from the transcriptional activator GCN4
    • Saudek V., Pasley H. S., Gibson T., Gausepohl H., Frank R., Pastore A. Solution structure of the basic region from the transcriptional activator GCN4. Biochemistry. 30:1991;1310-1317
    • (1991) Biochemistry , vol.30 , pp. 1310-1317
    • Saudek, V.1    Pasley, H.S.2    Gibson, T.3    Gausepohl, H.4    Frank, R.5    Pastore, A.6
  • 11
    • 0025155512 scopus 로고
    • Folding transition in the DNA-binding domain of GCN4 on specific binding to DNA
    • Weiss M. A., Ellenberger T., Wobbe C. R., Lee J. P., Harrison S. C., Struhl K. Folding transition in the DNA-binding domain of GCN4 on specific binding to DNA. Nature. 347:1990;575-578
    • (1990) Nature , vol.347 , pp. 575-578
    • Weiss, M.A.1    Ellenberger, T.2    Wobbe, C.R.3    Lee, J.P.4    Harrison, S.C.5    Struhl, K.6
  • 12
    • 0030821286 scopus 로고    scopus 로고
    • Specific DNA binding peptide derivatized solid support
    • Shin J. A. Specific DNA binding peptide derivatized solid support. Bioorg. Med. Chem. Lett. 7:1997;2367-2372
    • (1997) Bioorg. Med. Chem. Lett. , vol.7 , pp. 2367-2372
    • Shin, J.A.1
  • 13
    • 0024331502 scopus 로고
    • Cognate DNA binding specificity retained after leucine zipper exchange between GCN4 and C/EBP
    • Agre P., Johnson P. F., McKnight S. L. Cognate DNA binding specificity retained after leucine zipper exchange between GCN4 and C/EBP. Science. 246:1989;922-926
    • (1989) Science , vol.246 , pp. 922-926
    • Agre, P.1    Johnson, P.F.2    McKnight, S.L.3
  • 14
    • 85007648258 scopus 로고    scopus 로고
    • note
    • We use the C/EBP zipper because in related experiments, we covalently affix our proteins to solid support by diazotization through tyrosine; histidine may, however, interfere with the diazotization reaction. See Ref. 12. The GCN4 zipper contains a histidine, whereas the C/EBP zipper does not
  • 15
    • 0027432554 scopus 로고
    • Identification of C/EBP basic region residues involved in DNA sequence recognition and half-site spacing preference
    • Johnson P. F. Identification of C/EBP basic region residues involved in DNA sequence recognition and half-site spacing preference. Mol. Cell. Biol. 13:1993;6919-6930
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6919-6930
    • Johnson, P.F.1
  • 16
    • 0029916225 scopus 로고    scopus 로고
    • Control of aggregation in protein refolding: The temperature-leap tactic
    • Xie Y., Wetlaufer D. B. Control of aggregation in protein refolding: The temperature-leap tactic. Protein Science 5:1996;517-523
    • (1996) Protein Science , vol.5 , pp. 517-523
    • Xie, Y.1    Wetlaufer, D.B.2
  • 17
    • 0031573461 scopus 로고    scopus 로고
    • PCR-based gene synthesis and protein NMR spectroscopy
    • Casimiro D. R., Wright P. E., Dyson H. J. PCR-based gene synthesis and protein NMR spectroscopy. Structure. 5:1997;1407-1412
    • (1997) Structure , vol.5 , pp. 1407-1412
    • Casimiro, D.R.1    Wright, P.E.2    Dyson, H.J.3
  • 19
    • 0023473632 scopus 로고
    • The use of random-sequence oligonucleotides for determining consensus sequences
    • Oliphant A. R., Struhl K. The use of random-sequence oligonucleotides for determining consensus sequences. Methods Enzymol. 155:1987;568-582
    • (1987) Methods Enzymol. , vol.155 , pp. 568-582
    • Oliphant, A.R.1    Struhl, K.2
  • 20
    • 0022479114 scopus 로고
    • Cloning of random-sequence oligodeoxynucleotides
    • Oliphant A. R., Nussbaum A. L., Struhl K. Cloning of random-sequence oligodeoxynucleotides. Gene. 44:1986;177-183
    • (1986) Gene , vol.44 , pp. 177-183
    • Oliphant, A.R.1    Nussbaum, A.L.2    Struhl, K.3
  • 21
    • 0029027665 scopus 로고
    • Gene synthesis, high-level expression, and mutagenesis of Thiobacillus ferrooxidans rusticyanin: His 85 is a ligand to the blue copper center
    • Casimiro D. R., Toy-Palmer A., Blake R. C. II, Dyson H. J. Gene synthesis, high-level expression, and mutagenesis of Thiobacillus ferrooxidans rusticyanin: His 85 is a ligand to the blue copper center. Biochemistry. 34:1995;6640-6648
    • (1995) Biochemistry , vol.34 , pp. 6640-6648
    • Casimiro, D.R.1    Toy-Palmer, A.2    Blake, R.C.3    Dyson, H.J.4
  • 23
    • 0018846636 scopus 로고
    • Sequencing end-labelled DNA with base-specific chemical cleavages
    • Maxam A., Gilbert W. Sequencing end-labelled DNA with base-specific chemical cleavages. Methods Enzymol. 65:1980;499-560
    • (1980) Methods Enzymol. , vol.65 , pp. 499-560
    • Maxam, A.1    Gilbert, W.2
  • 24
    • 0028804911 scopus 로고
    • Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli
    • Kane J. F. Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli. Curr. Opin. Biotechnol. 6:1995;494-500
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 494-500
    • Kane, J.F.1
  • 25
    • 0019474499 scopus 로고
    • Correlation between the abundance of Escherichia coli transfer RNAs and the occurrence of the respective codons in its protein genes
    • Ikemura T. Correlation between the abundance of Escherichia coli transfer RNAs and the occurrence of the respective codons in its protein genes. J. Mol. Biol. 146:1981;1-21
    • (1981) J. Mol. Biol. , vol.146 , pp. 1-21
    • Ikemura, T.1
  • 26
    • 0026254055 scopus 로고
    • Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water
    • Scholtz J. M., Qian H., York E. J., Stewart J. M., Baldwin R. L. Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water. Biopolymers. 31:1991;1463-1470
    • (1991) Biopolymers , vol.31 , pp. 1463-1470
    • Scholtz, J.M.1    Qian, H.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 27
    • 0030046574 scopus 로고    scopus 로고
    • In vitro folding of inclusion body proteins
    • Rudolph R., Lilie H. In vitro folding of inclusion body proteins. FASEB J. 10:1996;49-56
    • (1996) FASEB J. , vol.10 , pp. 49-56
    • Rudolph, R.1    Lilie, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.