메뉴 건너뛰기




Volumn 80, Issue 1, 2011, Pages 47-51

A general method of protein purification for recombinant unstructured non-acidic proteins

Author keywords

Enzyme protection; Hydrophilins; Intrinsically unstructured proteins (IUPs); LEA proteins; Protein purification; TCA precipitation

Indexed keywords

ARABIDOPSIS PROTEIN; RECOMBINANT PROTEIN; TRICHLOROACETIC ACID;

EID: 80053301877     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2011.06.007     Document Type: Article
Times cited : (13)

References (36)
  • 4
    • 0034610396 scopus 로고    scopus 로고
    • Thermal behavior of proteins: Heat-resistant proteins and their heat-induced secondary structural changes
    • T.D. Kim, H.J. Ryu, H. Cho, C.-H. Yang, and J. Kim Thermal behavior of proteins: heat-resistant proteins and their heat-induced secondary structural changes Biochemistry 39 2000 14839 14846
    • (2000) Biochemistry , vol.39 , pp. 14839-14846
    • Kim, T.D.1    Ryu, H.J.2    Cho, H.3    Yang, C.-H.4    Kim, J.5
  • 5
    • 0033039345 scopus 로고    scopus 로고
    • Purification and assays for high mobility group HMG-I(Y) protein function
    • DOI 10.1016/S0076-6879(99)04011-2
    • R. Reeves, and M.S. Nissen Purification and assays for high mobility group HMG-I (Y) protein function Methods Enzymol. 304 1999 155 188 (Pubitemid 29268882)
    • (1999) Methods in Enzymology , vol.304 , pp. 155-188
    • Reeves, R.1    Nissen, M.S.2
  • 6
    • 26844566629 scopus 로고    scopus 로고
    • Uncovering the unfoldome: Enriching cell extracts for unstructured proteins by acid treatment
    • DOI 10.1021/pr050119c
    • M.S. Cortese, J.P. Baird, V.N. Uversky, and A.K. Dunker Uncovering the unfoldome: enriching cell extracts for unstructured proteins by acid treatment J. Proteome Res. 4 2005 1610 1618 (Pubitemid 41464787)
    • (2005) Journal of Proteome Research , vol.4 , Issue.5 , pp. 1610-1618
    • Cortese, M.S.1    Baird, J.P.2    Uversky, V.N.3    Dunker, A.K.4
  • 7
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • DOI 10.1038/nrm1589
    • H.J. Dyson, and P.E. Wright Intrinsically unstructured proteins and their functions Nat. Rev. Mol. Cell Biol. 6 2005 197 208 (Pubitemid 40314921)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 8
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • DOI 10.1016/j.febslet.2005.03.072, PII S0014579305004242
    • P. Tompa The interplay between structure and function in intrinsically unstructured proteins FEBS Lett. 579 2005 3346 3354 (Pubitemid 40804685)
    • (2005) FEBS Letters , vol.579 , Issue.15 , pp. 3346-3354
    • Tompa, P.1
  • 11
    • 34548460796 scopus 로고    scopus 로고
    • The continuing conundrum of the LEA proteins
    • DOI 10.1007/s00114-007-0254-y
    • A. Tunnacliffe, and M.J. Wise The continuing conundrum of the LEA proteins Naturwissenschaften 94 2007 791 812 (Pubitemid 47367664)
    • (2007) Naturwissenschaften , vol.94 , Issue.10 , pp. 791-812
    • Tunnacliffe, A.1    Wise, M.J.2
  • 13
    • 0034007384 scopus 로고    scopus 로고
    • Highly hydrophilic proteins in prokaryotes and eukaryotes are common during conditions of water deficit
    • DOI 10.1074/jbc.275.8.5668
    • A. Garay-Arroyo, J.M. Colmenero-Flores, A. Garciarrubio, and A.A. Covarrubias Highly hydrophilic proteins in prokaryotes and eukaryotes are common during conditions of water deficit J. Biol. Chem. 275 2000 5668 5674 (Pubitemid 30115206)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.8 , pp. 5668-5674
    • Garay-Arroyo, A.1    Colmenero-Flores, J.M.2    Garciarrubio, A.3    Covarrubias, A.A.4
  • 14
    • 77956706736 scopus 로고    scopus 로고
    • Functional analysis of the group 4 late embryogenesis abundant proteins reveals their relevance in the adaptive response during water deficit in Arabidopsis
    • Y. Olvera-Carrillo, F. Campos, J.L. Reyes, A. Garciarrubio, and Alejandra A. Covarrubias Functional analysis of the group 4 late embryogenesis abundant proteins reveals their relevance in the adaptive response during water deficit in Arabidopsis Plant Physiol. 154 2010 373 390
    • (2010) Plant Physiol. , vol.154 , pp. 373-390
    • Olvera-Carrillo, Y.1    Campos, F.2    Reyes, J.L.3    Garciarrubio, A.4    Covarrubias, A.A.5
  • 17
    • 17044405795 scopus 로고    scopus 로고
    • LEA proteins prevent protein aggregation due to water stress
    • DOI 10.1042/BJ20041931
    • K. Goyal, L.J. Walton, and L.J. Tunnacliffe LEA proteins prevent protein aggregation due to water stress Biochem. J. 388 2005 151 157 (Pubitemid 40732942)
    • (2005) Biochemical Journal , vol.388 , Issue.1 , pp. 151-157
    • Goyal, K.1    Walton, L.J.2    Tunnacliffe, A.3
  • 18
    • 0030021536 scopus 로고    scopus 로고
    • Expression of a late embryogenesis abundant protein gene, HVA1. from barley confers tolerance to water deficit and salt stress in transgenic rice
    • D. Xu, X. Duan, B. Wang, B. Hong, T.-H.D. Ho, and R. Wu Expression of a late embryogenesis abundant protein gene, HVA1. From barley confers tolerance to water deficit and salt stress in transgenic rice Plant Physiol. 110 1996 249 257
    • (1996) Plant Physiol. , vol.110 , pp. 249-257
    • Xu, D.1    Duan, X.2    Wang, B.3    Hong, B.4    Ho, T.-H.D.5    Wu, R.6
  • 19
    • 0036006031 scopus 로고    scopus 로고
    • Temperature-induced extended helix/random coil transitions in a group 1 late embryogenesis-abundant protein from soybean
    • DOI 10.1104/pp.010521
    • J.L. Soulages, K. Kim, C. Walters, and J.C. Cushman Temperature-induced extended helix/random coil transitions in a group 1 late embryogenesis-abundant protein from soybean Plant Physiol. 128 2002 822 832 (Pubitemid 34243820)
    • (2002) Plant Physiology , vol.128 , Issue.3 , pp. 822-832
    • Soulages, J.L.1    Kim, K.2    Walters, C.3    Cushman, J.C.4
  • 20
    • 0346034535 scopus 로고    scopus 로고
    • Conformation of a group 2 late embryogenesis abundant protein from soybean. Evidence of poly (L-proline)-type II structure
    • DOI 10.1104/pp.015891
    • J.L. Soulages, K. Kim, E.L. Arrese, C. Walters, and J.C. Cushman Conformation of a group 2 late embryogenesis abundant protein from soybean. Evidence of poly (L-proline)-type II structure Plant Physiol. 131 2003 963 975 (Pubitemid 36400336)
    • (2003) Plant Physiology , vol.131 , Issue.3 , pp. 963-975
    • Soulages, J.L.1    Kim, K.2    Arrese, E.L.3    Walters, C.4    Cushman, J.C.5
  • 21
    • 80052802440 scopus 로고    scopus 로고
    • Zinc induces disorder-to-order transitions in free and membrane-associated Thellungiellasalsuginea dehydrins TsDHN-1 and TsDHN-2: A solution CD and solid-state ATR-FTIR study
    • L.N. Rahman, V.V. Bamm, J.A.M. Voyer, G.S.T. Smith, L. Chen, M.W. Yaish, B.A. Moffatt, J.R. Dutcher, and G. Harauz Zinc induces disorder-to-order transitions in free and membrane-associated Thellungiellasalsuginea dehydrins TsDHN-1 and TsDHN-2: a solution CD and solid-state ATR-FTIR study Amino Acids 40 2011 1485 1502
    • (2011) Amino Acids , vol.40 , pp. 1485-1502
    • Rahman, L.N.1    Bamm, V.V.2    Voyer, J.A.M.3    Smith, G.S.T.4    Chen, L.5    Yaish, M.W.6    Moffatt, B.A.7    Dutcher, J.R.8    Harauz, G.9
  • 22
    • 70449521013 scopus 로고    scopus 로고
    • NMR assignments of the intrinsically disordered K2 and YSK2 dehydrins
    • E.E. Findlater, and S.P. Graether NMR assignments of the intrinsically disordered K2 and YSK2 dehydrins Biomol. NMR Assignments 3 2009 273 275
    • (2009) Biomol. NMR Assignments , vol.3 , pp. 273-275
    • Findlater, E.E.1    Graether, S.P.2
  • 23
    • 77949356529 scopus 로고    scopus 로고
    • Characterization of two soybean (Glycine max L.) LEA IV proteins by circular dichroism and Fourier transform infrared spectrometry
    • M.-D. Shih, T.-Y. Hsieh, T.-P. Lin, Y.-I.C. Hsing, and F.A. Hoekstra Characterization of two soybean (Glycine max L.) LEA IV proteins by circular dichroism and Fourier transform infrared spectrometry Plant Cell Physiol. 51 2010 395 407
    • (2010) Plant Cell Physiol. , vol.51 , pp. 395-407
    • Shih, M.-D.1    Hsieh, T.-Y.2    Lin, T.-P.3    Hsing, Y.-I.C.4    Hoekstra, F.A.5
  • 24
    • 33344476927 scopus 로고    scopus 로고
    • Two different late embryogenesis abundant proteins from Arabidopsis thaliana contain specific domains that inhibit Escherichia coli growth
    • DOI 10.1016/j.bbrc.2006.01.151, PII S0006291X06002191
    • F. Campos, F. Zamudio, and A.A. Covarrubias Two different late embryogenesis abundant proteins from Arabidopsis thaliana contain specific domains that inhibit Escherichia coli growth Biochem. Biophys. Res. Commun. 342 2006 406 413 (Pubitemid 43289008)
    • (2006) Biochemical and Biophysical Research Communications , vol.342 , Issue.2 , pp. 406-413
    • Campos, F.1    Zamudio, F.2    Covarrubias, A.A.3
  • 25
    • 33646874836 scopus 로고    scopus 로고
    • n-type dehydrin gene from bean in response to heavy metals
    • DOI 10.1385/MB:32:3:205
    • Y. Zhang, J. Li, F. Yu, L. Cong, L. Wang, G. Burkard, and T. Chai Cloning and expression analysis of SKn-type dehydrin gene from bean in response to heavy metals Mol. Biotechnol. 32 2006 205 217 (Pubitemid 43787132)
    • (2006) Molecular Biotechnology , vol.32 , Issue.3 , pp. 205-217
    • Zhang, Y.1    Li, J.2    Yu, F.3    Cong, L.4    Wang, L.5    Burkard, G.6    Chai, T.7
  • 26
    • 0032189932 scopus 로고    scopus 로고
    • Identification of sequence homology between the internal hydrophilic repeated motifs of Group 1 late-embryogenesis-abundant proteins in plants and hydrophilic repeats of the general stress protein GsiB of Bacillus subtilis
    • DOI 10.1007/s004250050424
    • R.A.P. Stacy, and R.B. Aalen Identification of sequence homology between the internal hydrophilic repeated motifs of group 1 late-embryogenesis abundant proteins in plants and hydrophilic repeats of the general stress protein GsiB of Bacillus subtilis Planta 206 1998 476 478 (Pubitemid 28422214)
    • (1998) Planta , vol.206 , Issue.3 , pp. 476-478
    • Stacy, R.A.P.1    Aalen, R.B.2
  • 27
    • 0023777735 scopus 로고
    • Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli
    • E. Amman, B. Ochs, and K. Abel Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli Gene 69 1988 301 315
    • (1988) Gene , vol.69 , pp. 301-315
    • Amman, E.1    Ochs, B.2    Abel, K.3
  • 28
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • S.C. Gill, and P.H. von Hippel Calculation of protein extinction coefficients from amino acid sequence data Anal. Biochem. 182 1989 319 326 (Pubitemid 19277112)
    • (1989) Analytical Biochemistry , vol.182 , Issue.2 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 29
    • 0038305931 scopus 로고    scopus 로고
    • Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein
    • DOI 10.1074/jbc.M212007200
    • K. Goyal, L. Tisi, A. Basran, J. Browne, A. Burnell, J. Zurdo, and A. Tunnacliffe Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein J. Biol. Chem. 278 2003 12977 12984 (Pubitemid 36800064)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.15 , pp. 12977-12984
    • Goyal, K.1    Tisi, L.2    Basran, A.3    Browne, J.4    Burnell, A.5    Zurdo, J.6    Tunnacliffe, A.7
  • 30
    • 78649776010 scopus 로고    scopus 로고
    • The intrinsically disordered late embryogenesis abundant protein LEA18 from Arabidopsis thaliana modulates membrane stability through binding and folding
    • M. Hundertmark, R. Dimova, J. Lengefeld, R. Seckler, and D.K. Hincha The intrinsically disordered late embryogenesis abundant protein LEA18 from Arabidopsis thaliana modulates membrane stability through binding and folding Biochim. Biophys. Acta 1808 2011 446 453
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 446-453
    • Hundertmark, M.1    Dimova, R.2    Lengefeld, J.3    Seckler, R.4    Hincha, D.K.5
  • 31
    • 36148995516 scopus 로고    scopus 로고
    • LC-MSMS identification of Arabidopsis thaliana heat-stable seed proteins: Enriching for LEA-type proteins by acid treatment
    • DOI 10.1002/jms.1292
    • E. Oliveira, I. Amera, D. Bellido, M.A. Odena, E. Domínguez, M. Pags, and A. Goday LC-MSMS identification of Arabidopsis thaliana heat-stable seed proteins: enriching for LEA-type proteins by acid treatment J. Mass Spectrom. 42 2007 1485 1495 (Pubitemid 350113466)
    • (2007) Journal of Mass Spectrometry , vol.42 , Issue.11 , pp. 1485-1495
    • Oliveira, E.1    Amara, I.2    Bellido, D.3    Odena, M.A.4    Dominguez, E.5    Pages, M.6    Goday, A.7
  • 32
    • 0033134023 scopus 로고    scopus 로고
    • Purification and partial characterization of a dehydrin involved in chilling tolerance during seedling emergence of cowpea
    • A.M. Ismail, A.E. Hall, and T.J. Close Purification and partial characterization of a dehydrin involved in chilling tolerance during seedling emergence of cowpea Plant Physiol. 120 1999 237 244 (Pubitemid 29375426)
    • (1999) Plant Physiology , vol.120 , Issue.1 , pp. 237-244
    • Ismail, A.M.1    Hall, A.E.2    Close, T.J.3
  • 33
    • 10644286555 scopus 로고    scopus 로고
    • β-Elimination coupled with tandem mass spectrometry for the identification of in vivo and in vitro phosphorylation sites in maize dehydrin DHN1 protein
    • DOI 10.1021/bi0483965
    • X. Jiang, and Y. Wang Β-elimination coupled with tandem mass spectrometry for the identification of in vivo and in vitro phosphorylation sites in maize dehydrin DHN1 protein Biochemistry 43 2004 15567 15576 (Pubitemid 39647482)
    • (2004) Biochemistry , vol.43 , Issue.49 , pp. 15567-15576
    • Jiang, X.1    Wang, Y.2
  • 34
    • 67649390736 scopus 로고    scopus 로고
    • Obtaining highly purified intrinsically disordered protein by boiling lysis and single step ion exchange
    • A.M. Livernois, D.J. Hnatchuk, E.E. Findlater, and S.P. Graether Obtaining highly purified intrinsically disordered protein by boiling lysis and single step ion exchange Anal. Biochem. 392 2009 70 76
    • (2009) Anal. Biochem. , vol.392 , pp. 70-76
    • Livernois, A.M.1    Hnatchuk, D.J.2    Findlater, E.E.3    Graether, S.P.4
  • 35
    • 0033769133 scopus 로고    scopus 로고
    • Purification of recombinant Arabidopsis thaliana dehydrins by metal ion affinity chromatography
    • J. Svensson, E.T. Palva, and B. Welin Purification of recombinant Arabidopsis thaliana dehydrins by metal ion affinity chromatography Protein Exp. Purif. 20 2000 169 178
    • (2000) Protein Exp. Purif. , vol.20 , pp. 169-178
    • Svensson, J.1    Palva, E.T.2    Welin, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.