메뉴 건너뛰기




Volumn , Issue SUPPL. 52, 2008, Pages

Recombinant protein complex expression in E. coli

Author keywords

Affinity tags; Multisubunit protein complexes; Polycistronic expression

Indexed keywords

BACTERIAL PROTEIN; PLASMID VECTOR; PROTEIN SUBUNIT; RECOMBINANT PROTEIN; TRANSFER RNA;

EID: 57549115264     PISSN: 19343655     EISSN: 19343663     Source Type: Journal    
DOI: 10.1002/0471140864.ps0521s52     Document Type: Review
Times cited : (39)

References (37)
  • 1
    • 33344478052 scopus 로고    scopus 로고
    • Regulation of yeast NRD1 expression by premature transcription termination
    • Arigo, J.T., Carroll, K.L., Ames, J.M., and Corden, J.L. 2006. Regulation of yeast NRD1 expression by premature transcription termination. Mol. Cell 21:641-651.
    • (2006) Mol. Cell , vol.21 , pp. 641-651
    • Arigo, J.T.1    Carroll, K.L.2    Ames, J.M.3    Corden, J.L.4
  • 2
    • 0037041022 scopus 로고    scopus 로고
    • Role of the Ada2 and Ada3 transcriptional coactivators in histone acetylation
    • Balasubramanian, R., Pray-Grant, M.G., Selleck, W., Grant, P.A., and Tan, S. 2002. Role of the Ada2 and Ada3 transcriptional coactivators in histone acetylation. J. Biol. Chem. 277:7989-7995.
    • (2002) J. Biol. Chem , vol.277 , pp. 7989-7995
    • Balasubramanian, R.1    Pray-Grant, M.G.2    Selleck, W.3    Grant, P.A.4    Tan, S.5
  • 3
    • 33847046355 scopus 로고    scopus 로고
    • Expression and purification of recombinant yeast Ada2/Ada3/Gcn5 and Piccolo NuA4 histone acetyltransferase complexes
    • Barrios, A., Selleck, W., Hnatkovich, B., Kramer, R., Sermwittayawong, D., and Tan, S. 2007. Expression and purification of recombinant yeast Ada2/Ada3/Gcn5 and Piccolo NuA4 histone acetyltransferase complexes. Methods 41:271-277.
    • (2007) Methods , vol.41 , pp. 271-277
    • Barrios, A.1    Selleck, W.2    Hnatkovich, B.3    Kramer, R.4    Sermwittayawong, D.5    Tan, S.6
  • 4
    • 0026327753 scopus 로고
    • A novel strategy for production of a highly expressed recombinant protein in an active form
    • Blackwell, J.R. and Horgan, R. 1991. A novel strategy for production of a highly expressed recombinant protein in an active form. FEBS Lett 295:10-12.
    • (1991) FEBS Lett , vol.295 , pp. 10-12
    • Blackwell, J.R.1    Horgan, R.2
  • 6
    • 0036809731 scopus 로고    scopus 로고
    • Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes
    • Boyer, L.A., Langer, M.R., Crowley, K.A., Tan, S., Denu, J.M., and Peterson, C.L. 2002. Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes. Mol. Cell 10:935-942.
    • (2002) Mol. Cell , vol.10 , pp. 935-942
    • Boyer, L.A.1    Langer, M.R.2    Crowley, K.A.3    Tan, S.4    Denu, J.M.5    Peterson, C.L.6
  • 7
    • 0024825088 scopus 로고
    • High-level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene product
    • Brinkmann, U., Mattes, R.E., and Buckel, P. 1989. High-level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene product. Gene 85:109-114.
    • (1989) Gene , vol.85 , pp. 109-114
    • Brinkmann, U.1    Mattes, R.E.2    Buckel, P.3
  • 8
    • 33847284995 scopus 로고    scopus 로고
    • Interaction of yeast RNA-binding proteins Nrd1 and Nab3 with RNA polymerase II terminator elements
    • Carroll, K.L., Ghirlando, R., Ames, J.M., and Corden, J.L. 2007. Interaction of yeast RNA-binding proteins Nrd1 and Nab3 with RNA polymerase II terminator elements. RNA 13:361-373.
    • (2007) RNA , vol.13 , pp. 361-373
    • Carroll, K.L.1    Ghirlando, R.2    Ames, J.M.3    Corden, J.L.4
  • 9
    • 33751232957 scopus 로고    scopus 로고
    • The conserved KMN network constitutes the core microtubule-binding site of the kinetochore
    • Cheeseman, I.M., Chappie, J.S., Wilson-Kubalek, E.M., and Desai, A. 2006. The conserved KMN network constitutes the core microtubule-binding site of the kinetochore. Cell 127:983-997.
    • (2006) Cell , vol.127 , pp. 983-997
    • Cheeseman, I.M.1    Chappie, J.S.2    Wilson-Kubalek, E.M.3    Desai, A.4
  • 10
    • 1342346531 scopus 로고    scopus 로고
    • Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans
    • Doyon, Y., Selleck, W., Lane, W.S., Tan, S., and Cote, J. 2004. Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans. Mol. Cell Biol. 24:1884-1896.
    • (2004) Mol. Cell Biol , vol.24 , pp. 1884-1896
    • Doyon, Y.1    Selleck, W.2    Lane, W.S.3    Tan, S.4    Cote, J.5
  • 11
  • 12
    • 0035895435 scopus 로고    scopus 로고
    • Dissecting the interaction network of multiprotein complexes by pairwise coexpression of subunits in E. coli
    • Fribourg, S., Romier, C., Werten, S., Gangloff, Y.G., Poterszman, A., and Moras, D. 2001. Dissecting the interaction network of multiprotein complexes by pairwise coexpression of subunits in E. coli. J. Mol. Biol. 306:363-373.
    • (2001) J. Mol. Biol , vol.306 , pp. 363-373
    • Fribourg, S.1    Romier, C.2    Werten, S.3    Gangloff, Y.G.4    Poterszman, A.5    Moras, D.6
  • 13
    • 0028245269 scopus 로고
    • Recombinant replication protein A: Expression, complex formation, and functional characterization
    • Henricksen, L.A., Umbricht, C.B., and Wold, M.S. 1994. Recombinant replication protein A: Expression, complex formation, and functional characterization. J. Biol. Chem. 269:11121-11132.
    • (1994) J. Biol. Chem , vol.269 , pp. 11121-11132
    • Henricksen, L.A.1    Umbricht, C.B.2    Wold, M.S.3
  • 15
    • 0029833905 scopus 로고    scopus 로고
    • Purification, gene cloning, and reconstitution of the heterotrimeric single-stranded DNA-binding protein from Schizosac-charomyces pombe
    • Ishiai, M., Sanchez, J.P., Amin, A.A., Murakami, Y., and Hurwitz, J. 1996. Purification, gene cloning, and reconstitution of the heterotrimeric single-stranded DNA-binding protein from Schizosac-charomyces pombe. J. Biol. Chem. 271:20868-20878.
    • (1996) J. Biol. Chem , vol.271 , pp. 20868-20878
    • Ishiai, M.1    Sanchez, J.P.2    Amin, A.A.3    Murakami, Y.4    Hurwitz, J.5
  • 16
    • 0033662861 scopus 로고    scopus 로고
    • Coexpression of proteins in bacteria using T7-based expression plasmids: Expression of heteromeric cell-cycle and transcriptional regulatory complexes
    • Johnston, K., Clements, A., Venkataramani, R.N., Trievel, R.C., and Marmorstein, R. 2000. Coexpression of proteins in bacteria using T7-based expression plasmids: Expression of heteromeric cell-cycle and transcriptional regulatory complexes. Protein Expr. Purif. 20:435-443.
    • (2000) Protein Expr. Purif , vol.20 , pp. 435-443
    • Johnston, K.1    Clements, A.2    Venkataramani, R.N.3    Trievel, R.C.4    Marmorstein, R.5
  • 19
    • 0030938085 scopus 로고    scopus 로고
    • Coexpression of nuclear receptor partners increases their solubility and biological activities
    • Li, C., Schwabe, J.W., Banayo, E., and Evans, R.M. 1997. Coexpression of nuclear receptor partners increases their solubility and biological activities. Proc. Natl. Acad. Sci. U.S.A. 94:2278-2283.
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 2278-2283
    • Li, C.1    Schwabe, J.W.2    Banayo, E.3    Evans, R.M.4
  • 21
    • 0031587289 scopus 로고    scopus 로고
    • Characterization of nucleosome core particles containing histone proteins made in bacteria
    • Luger, K., Rechsteiner, T.J., Flaus, A.J., Waye, M.M., and Richmond, T.J. 1997. Characterization of nucleosome core particles containing histone proteins made in bacteria. J. Mol. Biol. 272:301-311.
    • (1997) J. Mol. Biol , vol.272 , pp. 301-311
    • Luger, K.1    Rechsteiner, T.J.2    Flaus, A.J.3    Waye, M.M.4    Richmond, T.J.5
  • 22
    • 2042515635 scopus 로고
    • Coexpression and assembly of myosin heavy chain and myosin light chain in Escherichia coli
    • McNally, E.M., Goodwin, E.B., Spudich, J.A., and Leinwand, L.A. 1988. Coexpression and assembly of myosin heavy chain and myosin light chain in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 85:7270-7273.
    • (1988) Proc. Natl. Acad. Sci. U.S.A , vol.85 , pp. 7270-7273
    • McNally, E.M.1    Goodwin, E.B.2    Spudich, J.A.3    Leinwand, L.A.4
  • 23
    • 33744970012 scopus 로고    scopus 로고
    • The CENP-H-I complex is required for the efficient incorporation of newly synthesized CENP-A into centromeres
    • Okada, M., Cheeseman, I.M., Hori, T., Okawa K., McLeod, I.X., Yates, J.R., 3rd, Desai, A., and Fukagawa, T. 2006. The CENP-H-I complex is required for the efficient incorporation of newly synthesized CENP-A into centromeres. Nat. Cell Biol. 8:446-457.
    • (2006) Nat. Cell Biol , vol.8 , pp. 446-457
    • Okada, M.1    Cheeseman, I.M.2    Hori, T.3    Okawa, K.4    McLeod, I.X.5    Yates 3rd, J.R.6    Desai, A.7    Fukagawa, T.8
  • 24
    • 0028329918 scopus 로고
    • Release of proteins and peptides from fusion proteins using a recombinant plant virus proteinase
    • Parks, T.D., Leuther, K.K., Howard, E.D., Johnston, S.A., and Dougherty, W.G. 1994. Release of proteins and peptides from fusion proteins using a recombinant plant virus proteinase. Anal. Biochem. 216:413-417.
    • (1994) Anal. Biochem , vol.216 , pp. 413-417
    • Parks, T.D.1    Leuther, K.K.2    Howard, E.D.3    Johnston, S.A.4    Dougherty, W.G.5
  • 25
    • 0034841844 scopus 로고    scopus 로고
    • The tandem affinity purification (TAP) method: A general procedure of protein complex purification
    • Puig, O., Caspary, F., Rigaut, G., Rutz, B., Bouveret, E., Bragado-Nilsson, E., Wilm, M., and Seraphin, B. 2001. The tandem affinity purification (TAP) method: A general procedure of protein complex purification. Methods 24:218-229.
    • (2001) Methods , vol.24 , pp. 218-229
    • Puig, O.1    Caspary, F.2    Rigaut, G.3    Rutz, B.4    Bouveret, E.5    Bragado-Nilsson, E.6    Wilm, M.7    Seraphin, B.8
  • 26
    • 0029767016 scopus 로고    scopus 로고
    • Structural basis of cyclin-dependent kinase activation by phosphorylation
    • Russo, A.A., Jeffrey, P.D., and Pavletich, N.P. 1996. Structural basis of cyclin-dependent kinase activation by phosphorylation. Nat. Struct. Biol. 3:696-700.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 696-700
    • Russo, A.A.1    Jeffrey, P.D.2    Pavletich, N.P.3
  • 27
    • 0023892436 scopus 로고
    • Formation of soluble recombinant proteins in Escherichia coli is favored by lower growth temperature
    • Schein, C.H. and Noteborn, M.H.M. 1988. Formation of soluble recombinant proteins in Escherichia coli is favored by lower growth temperature. Bio/Technology 6:291-294.
    • (1988) Bio/Technology , vol.6 , pp. 291-294
    • Schein, C.H.1    Noteborn, M.H.M.2
  • 28
    • 20744445493 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Piccolo NuA4 histone acetyltransferase complex requires the Enhancer of Polycomb A domain and chromodomain to acetylate nucleosomes
    • Selleck, W., Fortin, I., Sermwittayawong, D., Cote, J., and Tan, S. 2005. The Saccharomyces cerevisiae Piccolo NuA4 histone acetyltransferase complex requires the Enhancer of Polycomb A domain and chromodomain to acetylate nucleosomes. Mol. Cell Biol. 25:5535-5542.
    • (2005) Mol. Cell Biol , vol.25 , pp. 5535-5542
    • Selleck, W.1    Fortin, I.2    Sermwittayawong, D.3    Cote, J.4    Tan, S.5
  • 30
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier, F.W. 2005. Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif. 41:207-234.
    • (2005) Protein Expr. Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 32
    • 0034963119 scopus 로고    scopus 로고
    • A modular polycistronic expression system for overexpressing protein complexes in Escherichia coli
    • Tan, S. 2001. A modular polycistronic expression system for overexpressing protein complexes in Escherichia coli. Protein Expr. Purif. 21:224-234.
    • (2001) Protein Expr. Purif , vol.21 , pp. 224-234
    • Tan, S.1
  • 33
    • 0029870514 scopus 로고    scopus 로고
    • Crystal structure of a yeast TFIIA/TBP/DNA complex
    • Tan, S., Hunziker, Y., Sargent, D.F., and Richmond, T.J. 1996. Crystal structure of a yeast TFIIA/TBP/DNA complex. Nature 381:127-151.
    • (1996) Nature , vol.381 , pp. 127-151
    • Tan, S.1    Hunziker, Y.2    Sargent, D.F.3    Richmond, T.J.4
  • 34
    • 14844303376 scopus 로고    scopus 로고
    • The pST44 polycistronic expression system for producing protein complexes in E. coli
    • Tan, S., Kern, R.C., and Selleck, W. 2005. The pST44 polycistronic expression system for producing protein complexes in E. coli. Protein Expr. Purif. 40:385-395.
    • (2005) Protein Expr. Purif , vol.40 , pp. 385-395
    • Tan, S.1    Kern, R.C.2    Selleck, W.3
  • 35
    • 0033010723 scopus 로고    scopus 로고
    • Reconstitution of the transcription factor TFIIH: Assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7
    • Tirode, F., Busso, D., Coin, F., and Egly, J.M. 1999. Reconstitution of the transcription factor TFIIH: Assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7. Mol. Cell 3:87-95.
    • (1999) Mol. Cell , vol.3 , pp. 87-95
    • Tirode, F.1    Busso, D.2    Coin, F.3    Egly, J.M.4
  • 36
    • 0028793115 scopus 로고
    • Increase of solubility of foreign proteins in Escherichia coli by coproduction of the bacterial thioredoxin
    • Yasukawa, T., Kanei-Ishii, C., Maekawa, T., Fujimoto, J., Yamamoto, T., and Ishii, S. 1995. Increase of solubility of foreign proteins in Escherichia coli by coproduction of the bacterial thioredoxin. J. Biol. Chem. 270:25328-25331.
    • (1995) J. Biol. Chem , vol.270 , pp. 25328-25331
    • Yasukawa, T.1    Kanei-Ishii, C.2    Maekawa, T.3    Fujimoto, J.4    Yamamoto, T.5    Ishii, S.6
  • 37
    • 0025286302 scopus 로고
    • Recombinant RNA polymerase: Inducible overexpression, purification and assembly of Escherichia coli rpo gene products
    • Zalenskaya, K., Lee, J., Gujuluva, C.N., Shin, Y.K., Slutsky, M., and Goldfarb, A. 1990. Recombinant RNA polymerase: Inducible overexpression, purification and assembly of Escherichia coli rpo gene products. Gene 89:7-12.
    • (1990) Gene , vol.89 , pp. 7-12
    • Zalenskaya, K.1    Lee, J.2    Gujuluva, C.N.3    Shin, Y.K.4    Slutsky, M.5    Goldfarb, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.