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Maltose-binding protein

April 11, 2024

Maltose-binding protein (MBP) is a part of the maltose/maltodextrin system of Escherichia coli, which is responsible for the uptake and efficient catabolism of maltodextrins. It is a complex regulatory and transport system involving many proteins and protein complexes. MBP has an approximate molecular mass of 42.5 kilodaltons.

Maltose/maltodextrin-binding periplasmic protein
Maltose-binding protein from Escherichia coli, with a bound sugar molecule shown as red spheres, from PDB: 1FQC​.[1]
Identifiers
OrganismEscherichia coli
SymbolMalE
UniProtP0AEX9
Search for
StructuresSwiss-model
DomainsInterPro

Structure and folding edit

MBP is encoded by the malE gene of Escherichia coli. The malE gene codes for a precursor polypeptide (396 amino acid residues) which yields the mature MBP (370 residues) upon cleavage of the NH2-terminal extension (26 residues). The precursor and mature forms of MBP do not contain any cysteine residues.[2]

MBP is a monomeric protein. Crystal structures have shown that MBP is divided into two distinct globular domains that are connected by three short polypeptide segments. The two domains are separated by a deep groove that contains the maltose/maltodextrin binding site. Comparison of the structures of the liganded and unliganded forms of MBP has shown that the binding of maltose induces a major conformational change that closes the groove by a rigid motion of the two domains around the linking polypeptide hinge.[3][4]

Both precursor and mature forms of MBP are functional for the binding of maltose.[5] The NH2-terminal extension decreases the folding rate of the precursor form of MBP relative to its mature form by at least 5 fold, but it has no effect on the unfolding rate.[6][7] The equilibrium unfolding of MBP can be modelled by a two-state mechanism with a stability ∆G(H2O) equal to 9.45 kcal mol−1 at 25 °C, pH 7.6.[8]

Localization and export edit

MBP is exported into the periplasmic space of E. coli.[9] The NH2-terminal extension of MBP, also termed signal peptide, has two roles: (i) it slows down folding of the newly synthesized polypeptide, and (ii) it directs this polypeptide to the membrane and SecYEG translocon. Once folded, the precursor can no longer enter the translocation pathway.[10] The introduction of a charged amino-acid residue or a proline residue within the hydrophobic core of the signal peptide is sufficient to block export.[11] The defective exports of the mutant MBPs are consistent with the alpha-helical conformation and hydrophobic interactions of the signal peptide in its interaction with the translocon motor protein SecA.[12][13][14]

Control of expression edit

The malE gene, coding for MBP, belongs to the Mal regulon of E. coli, which consists of ten genes whose products are geared for the efficient uptake and utilization of maltose and maltodextrins. All the gene involved in the transport of maltose/maltodextrin, including malE, are clustered in the malB region of E. coli and organized in two divergent operons: malE-malF-malG and malK-lamB.[15] The transcription start sites at the malEp and malKp promoters are distant of 271 base pairs.[16]

The malEp and malKp promoters are synergistically activated by protein MalT, the activator of the Mal regulon and by the cAMP receptor protein CRP. This activation is a coupled process that involves, going from malEp towards malKp: two MalT binding sites; three CRP binding site, and two overlapping sets of three MalT binding sites, staggered by three base pairs.[16][17][18] Transcription activation requires the binding of adenosine triphosphate (ATP) and maltotriose to MalT and the binding of cyclic AMP to the dimer of CRP.[19] The unliganded form of MalT is monomeric whereas its liganded form, in the presence of ATP and maltotriose, is oligomeric.[20]

Use as a protein and peptide vector edit

MBP is used to increase the solubility of recombinant proteins expressed in E. coli. In these systems, the protein of interest is often expressed as a MBP-fusion protein, preventing aggregation of the protein of interest. The mechanism by which MBP increases solubility is not well understood. In addition, MBP can itself be used as an affinity tag for purification of recombinant proteins. The fusion protein binds to amylose columns while all other proteins flow through. The MBP-protein fusion can be purified by eluting the column with maltose. Once the fusion protein is obtained in purified form, the protein of interest is often cleaved from MBP with a specific protease and can then be separated from MBP by affinity chromatography.

A first study of the relations between structure and functions of MBP was performed by random insertion of a short DNA fragment, coding for a BamHI restriction site, into the malE gene. Some of the insertions affected the functions of MBP whereas others were permissive.[21][22] The permissive sites that were internal to MBP, were used to insert antigenic peptides and challenge the immune response in mice.[23] The 3'-OH terminal insertions were used to create fusion proteins and develop the use of MBP as an affinity handle for the purification of foreign proteins and peptides by affinity chromatography on cross-linked amylose and elution with maltose in mild physico-chemical conditions.[24][25] Several plasmid vectors were developed to facilitate the expression and purification of such fusion proteins.[26]

When the recombinant MBP includes a signal peptide, the fusion protein can be exported into the periplasmic space, which facilitate its purification since the periplasmic fluid contains only a limited number of proteins and can be recovered either by an osmotic shock or by permeabilization of the bacterial outer membrane with antibiotics such as Polymyxin B. Such an export of the fusion protein into the periplasmic space enables the formation of disulfide bonds in the passenger protein, for example antibody fragments.[27][28] Foreign proteins that are exported or secreted in their native organism, can usually be exported into the E. coli periplasm by fusion with MBP. Examples of cytoplasmic proteins that could be exported by fusion with MBP, include the monomeric Klenow polymerase and the dimeric Gene V protein of phage M13.[24][29] When the recombinant MBP includes either a defective or no signal peptide the fusion protein remains within the bacterial cytoplasm from where it can be recovered by breaking open the cells.

The fusion of proteins with MBP usually enhances their solubility and facilitates their proper folding so that the fusion proteins are most often bifunctional.[24][30] In addition, such fusions can facilitate the crystallisation of difficult proteins, e.g. membrane proteins. The crystallized protein can often have their structures solved by X-ray crystallography using molecular replacement on a known MBP structure.[31]

See also edit

References edit

  1. ^ Duan, Xiaoqun; Hall, Jason A; Nikaido, Hiroshi; Quiocho, Florante A (March 2001). "Crystal structures of the maltodextrin/maltose-binding protein complexed with reduced oligosaccharides: flexibility of tertiary structure and ligand binding". Journal of Molecular Biology. 306 (5): 1115–1126. doi:10.1006/jmbi.2001.4456. PMID 11237621.
  2. ^ Duplay P, Bedouelle H, Fowler A, Zabin I, Saurin W, Hofnung M (August 1984). "Sequences of the malE gene and of its product, the maltose-binding protein of Escherichia coli K12". The Journal of Biological Chemistry. 259 (16): 10606–13. doi:10.1016/S0021-9258(18)91005-7. PMID 6088507.
  3. ^ Spurlino JC, Lu GY, Quiocho FA (March 1991). "The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis". The Journal of Biological Chemistry. 266 (8): 5202–19. doi:10.2210/pdb1mbp/pdb. PMID 2002054.
  4. ^ Sharff AJ, Rodseth LE, Spurlino JC, Quiocho FA (November 1992). "Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis". Biochemistry. 31 (44): 10657–63. doi:10.1021/bi00159a003. PMID 1420181.
  5. ^ Ferenci T, Randall LL (October 1979). "Precursor maltose-binding protein is active in binding substrate". The Journal of Biological Chemistry. 254 (20): 9979–81. doi:10.1016/S0021-9258(19)86659-0. PMID 385604.
  6. ^ Park S, Liu G, Topping TB, Cover WH, Randall LL (February 1988). "Modulation of folding pathways of exported proteins by the leader sequence". Science. 239 (4843): 1033–5. Bibcode:1988Sci...239.1033P. doi:10.1126/science.3278378. PMID 3278378.
  7. ^ Beena K, Udgaonkar JB, Varadarajan R (March 2004). "Effect of signal peptide on the stability and folding kinetics of maltose binding protein". Biochemistry. 43 (12): 3608–19. doi:10.1021/bi0360509. PMID 15035631.
  8. ^ Chun SY, Strobel S, Bassford P, Randall LL (October 1993). "Folding of maltose-binding protein. Evidence for the identity of the rate-determining step in vivo and in vitro". The Journal of Biological Chemistry. 268 (28): 20855–62. doi:10.1016/S0021-9258(19)36864-4. PMID 8407916.
  9. ^ Kellermann O, Szmelcman S (August 1974). "Active transport of maltose in Escherichia coli K12. Involvement of a "periplasmic" maltose binding protein". European Journal of Biochemistry. 47 (1): 139–49. doi:10.1111/j.1432-1033.1974.tb03677.x. PMID 4215651.
  10. ^ Randall LL, Hardy SJ (September 1986). "Correlation of competence for export with lack of tertiary structure of the mature species: a study in vivo of maltose-binding protein in E. coli". Cell. 46 (6): 921–8. doi:10.1016/0092-8674(86)90074-7. PMID 3530497. S2CID 28503725.
  11. ^ Bedouelle H, Bassford PJ, Fowler AV, Zabin I, Beckwith J, Hofnung M (May 1980). "Mutations which alter the function of the signal sequence of the maltose binding protein of Escherichia coli". Nature. 285 (5760): 78–81. Bibcode:1980Natur.285...78B. doi:10.1038/285078a0. PMID 6990274. S2CID 4253747.
  12. ^ Bedouelle H, Hofnung M (1981). "Functional implications of secondary structure analysis of wild type and mutant bacterial signal peptides". Progress in Clinical and Biological Research. 63: 399–403. PMID 7312870.
  13. ^ Chou YT, Gierasch LM (September 2005). "The conformation of a signal peptide bound by Escherichia coli preprotein translocase SecA". The Journal of Biological Chemistry. 280 (38): 32753–60. doi:10.1074/jbc.M507532200. PMID 16046390.
  14. ^ Gelis I, Bonvin AM, Keramisanou D, Koukaki M, Gouridis G, Karamanou S, Economou A, Kalodimos CG (November 2007). "Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR". Cell. 131 (4): 756–69. doi:10.1016/j.cell.2007.09.039. PMC 2170882. PMID 18022369.
  15. ^ Boos W, Shuman H (March 1998). "Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation". Microbiology and Molecular Biology Reviews. 62 (1): 204–29. doi:10.1128/MMBR.62.1.204-229.1998. PMC 98911. PMID 9529892.
  16. ^ a b Bedouelle H, Schmeissner U, Hofnung M, Rosenberg M (November 1982). "Promoters of the malEFG and malK-lamB operons in Escherichia coli K12". Journal of Molecular Biology. 161 (4): 519–31. doi:10.1016/0022-2836(82)90405-3. PMID 6185687.
  17. ^ Bedouelle H (November 1983). "Mutations in the promoter regions of the malEFG and malK-lamB operons of Escherichia coli K12". Journal of Molecular Biology. 170 (4): 861–82. doi:10.1016/s0022-2836(83)80192-2. PMID 6417341.
  18. ^ Richet E (October 2000). "Synergistic transcription activation: a dual role for CRP in the activation of an Escherichia coli promoter depending on MalT and CRP". The EMBO Journal. 19 (19): 5222–32. doi:10.1093/emboj/19.19.5222. PMC 302108. PMID 11013224.
  19. ^ Richet E, Raibaud O (March 1989). "MalT, the regulatory protein of the Escherichia coli maltose system, is an ATP-dependent transcriptional activator". The EMBO Journal. 8 (3): 981–7. doi:10.1002/j.1460-2075.1989.tb03461.x. PMC 400900. PMID 2524384.
  20. ^ Schreiber V, Richet E (November 1999). "Self-association of the Escherichia coli transcription activator MalT in the presence of maltotriose and ATP". The Journal of Biological Chemistry. 274 (47): 33220–6. doi:10.1074/jbc.274.47.33220. PMID 10559195.
  21. ^ Duplay P, Bedouelle H, Szmelcman S, Hofnung M (1985). "Linker mutagenesis in the gene encoding the periplasmic maltose-binding protein of E. coli". Biochimie. 67 (7–8): 849–51. doi:10.1016/s0300-9084(85)80178-4. PMID 3002495.
  22. ^ Duplay P, Szmelcman S, Bedouelle H, Hofnung M (April 1987). "Silent and functional changes in the periplasmic maltose-binding protein of Escherichia coli K12. I. Transport of maltose". Journal of Molecular Biology. 194 (4): 663–73. doi:10.1016/0022-2836(87)90243-9. PMID 2821264.
  23. ^ Coëffier E, Clément JM, Cussac V, Khodaei-Boorane N, Jehanno M, Rojas M, Dridi A, Latour M, El Habib R, Barré-Sinoussi F, Hofnung M, Leclerc C (November 2000). "Antigenicity and immunogenicity of the HIV-1 gp41 epitope ELDKWA inserted into permissive sites of the MalE protein". Vaccine. 19 (7–8): 684–93. doi:10.1016/s0264-410x(00)00267-x. PMID 11115689.
  24. ^ a b c Bedouelle H, Duplay P (February 1988). "Production in Escherichia coli and one-step purification of bifunctional hybrid proteins which bind maltose. Export of the Klenow polymerase into the periplasmic space". European Journal of Biochemistry. 171 (3): 541–9. doi:10.1111/j.1432-1033.1988.tb13823.x. PMID 3278900.
  25. ^ Rondard P, Brégégère F, Lecroisey A, Delepierre M, Bedouelle H (July 1997). "Conformational and functional properties of an undecapeptide epitope fused with the C-terminal end of the maltose binding protein". Biochemistry. 36 (29): 8954–61. CiteSeerX 10.1.1.599.2650. doi:10.1021/bi962508d. PMID 9220983.
  26. ^ di Guan C, Li P, Riggs PD, Inouye H (July 1988). "Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein". Gene. 67 (1): 21–30. doi:10.1016/0378-1119(88)90004-2. PMID 2843437.
  27. ^ Brégégère F, Schwartz J, Bedouelle H (February 1994). "Bifunctional hybrids between the variable domains of an immunoglobulin and the maltose-binding protein of Escherichia coli: production, purification and antigen binding". Protein Engineering. 7 (2): 271–80. PMID 8170930.
  28. ^ Malik A (June 2016). "Protein fusion tags for efficient expression and purification of recombinant proteins in the periplasmic space of E. coli". 3 Biotech. 6 (1): 44. doi:10.1007/s13205-016-0397-7. PMC 4742420. PMID 28330113.
  29. ^ Blondel A, Bedouelle H (October 1990). "Export and purification of a cytoplasmic dimeric protein by fusion to the maltose-binding protein of Escherichia coli". European Journal of Biochemistry. 193 (2): 325–30. doi:10.1111/j.1432-1033.1990.tb19341.x. PMID 2226455.
  30. ^ Kapust RB, Waugh DS (August 1999). "Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused". Protein Science. 8 (8): 1668–74. doi:10.1110/ps.8.8.1668. PMC 2144417. PMID 10452611.
  31. ^ Waugh DS (March 2016). "Crystal structures of MBP fusion proteins". Protein Science. 25 (3): 559–71. doi:10.1002/pro.2863. PMC 4815407. PMID 26682969.

External links edit

  • N-Terminal Fusion of Target Protein to Maltose-Binding Protein at Michigan Technological University
  • maltose-binding+protein at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
  • Generic protocol for the expression and purification of recombinant proteins in Escherichia coli using a combinatorial His6-maltose binding protein fusion tag

April 11, 2024
maltose, binding, protein, part, maltose, maltodextrin, system, escherichia, coli, which, responsible, uptake, efficient, catabolism, maltodextrins, complex, regulatory, transport, system, involving, many, proteins, protein, complexes, approximate, molecular, . Maltose binding protein MBP is a part of the maltose maltodextrin system of Escherichia coli which is responsible for the uptake and efficient catabolism of maltodextrins It is a complex regulatory and transport system involving many proteins and protein complexes MBP has an approximate molecular mass of 42 5 kilodaltons Maltose maltodextrin binding periplasmic proteinMaltose binding protein from Escherichia coli with a bound sugar molecule shown as red spheres from PDB 1FQC 1 IdentifiersOrganismEscherichia coliSymbolMalEUniProtP0AEX9Search forStructuresSwiss modelDomainsInterPro Contents 1 Structure and folding 2 Localization and export 3 Control of expression 4 Use as a protein and peptide vector 5 See also 6 References 7 External linksStructure and folding editMBP is encoded by the malE gene of Escherichia coli The malE gene codes for a precursor polypeptide 396 amino acid residues which yields the mature MBP 370 residues upon cleavage of the NH2 terminal extension 26 residues The precursor and mature forms of MBP do not contain any cysteine residues 2 MBP is a monomeric protein Crystal structures have shown that MBP is divided into two distinct globular domains that are connected by three short polypeptide segments The two domains are separated by a deep groove that contains the maltose maltodextrin binding site Comparison of the structures of the liganded and unliganded forms of MBP has shown that the binding of maltose induces a major conformational change that closes the groove by a rigid motion of the two domains around the linking polypeptide hinge 3 4 Both precursor and mature forms of MBP are functional for the binding of maltose 5 The NH2 terminal extension decreases the folding rate of the precursor form of MBP relative to its mature form by at least 5 fold but it has no effect on the unfolding rate 6 7 The equilibrium unfolding of MBP can be modelled by a two state mechanism with a stability G H2O equal to 9 45 kcal mol 1 at 25 C pH 7 6 8 Localization and export editMBP is exported into the periplasmic space of E coli 9 The NH2 terminal extension of MBP also termed signal peptide has two roles i it slows down folding of the newly synthesized polypeptide and ii it directs this polypeptide to the membrane and SecYEG translocon Once folded the precursor can no longer enter the translocation pathway 10 The introduction of a charged amino acid residue or a proline residue within the hydrophobic core of the signal peptide is sufficient to block export 11 The defective exports of the mutant MBPs are consistent with the alpha helical conformation and hydrophobic interactions of the signal peptide in its interaction with the translocon motor protein SecA 12 13 14 Control of expression editThe malE gene coding for MBP belongs to the Mal regulon of E coli which consists of ten genes whose products are geared for the efficient uptake and utilization of maltose and maltodextrins All the gene involved in the transport of maltose maltodextrin including malE are clustered in the malB region of E coli and organized in two divergent operons malE malF malG and malK lamB 15 The transcription start sites at the malEp and malKp promoters are distant of 271 base pairs 16 The malEp and malKp promoters are synergistically activated by protein MalT the activator of the Mal regulon and by the cAMP receptor protein CRP This activation is a coupled process that involves going from malEp towards malKp two MalT binding sites three CRP binding site and two overlapping sets of three MalT binding sites staggered by three base pairs 16 17 18 Transcription activation requires the binding of adenosine triphosphate ATP and maltotriose to MalT and the binding of cyclic AMP to the dimer of CRP 19 The unliganded form of MalT is monomeric whereas its liganded form in the presence of ATP and maltotriose is oligomeric 20 Use as a protein and peptide vector editMBP is used to increase the solubility of recombinant proteins expressed in E coli In these systems the protein of interest is often expressed as a MBP fusion protein preventing aggregation of the protein of interest The mechanism by which MBP increases solubility is not well understood In addition MBP can itself be used as an affinity tag for purification of recombinant proteins The fusion protein binds to amylose columns while all other proteins flow through The MBP protein fusion can be purified by eluting the column with maltose Once the fusion protein is obtained in purified form the protein of interest is often cleaved from MBP with a specific protease and can then be separated from MBP by affinity chromatography A first study of the relations between structure and functions of MBP was performed by random insertion of a short DNA fragment coding for a BamHI restriction site into the malE gene Some of the insertions affected the functions of MBP whereas others were permissive 21 22 The permissive sites that were internal to MBP were used to insert antigenic peptides and challenge the immune response in mice 23 The 3 OH terminal insertions were used to create fusion proteins and develop the use of MBP as an affinity handle for the purification of foreign proteins and peptides by affinity chromatography on cross linked amylose and elution with maltose in mild physico chemical conditions 24 25 Several plasmid vectors were developed to facilitate the expression and purification of such fusion proteins 26 When the recombinant MBP includes a signal peptide the fusion protein can be exported into the periplasmic space which facilitate its purification since the periplasmic fluid contains only a limited number of proteins and can be recovered either by an osmotic shock or by permeabilization of the bacterial outer membrane with antibiotics such as Polymyxin B Such an export of the fusion protein into the periplasmic space enables the formation of disulfide bonds in the passenger protein for example antibody fragments 27 28 Foreign proteins that are exported or secreted in their native organism can usually be exported into the E coli periplasm by fusion with MBP Examples of cytoplasmic proteins that could be exported by fusion with MBP include the monomeric Klenow polymerase and the dimeric Gene V protein of phage M13 24 29 When the recombinant MBP includes either a defective or no signal peptide the fusion protein remains within the bacterial cytoplasm from where it can be recovered by breaking open the cells The fusion of proteins with MBP usually enhances their solubility and facilitates their proper folding so that the fusion proteins are most often bifunctional 24 30 In addition such fusions can facilitate the crystallisation of difficult proteins e g membrane proteins The crystallized protein can often have their structures solved by X ray crystallography using molecular replacement on a known MBP structure 31 See also editProtein tag Fluorescent glucose biosensors Glutathione S transferaseReferences edit Duan Xiaoqun Hall Jason A Nikaido Hiroshi Quiocho Florante A March 2001 Crystal structures of the maltodextrin maltose binding protein complexed with reduced oligosaccharides flexibility of tertiary structure and ligand binding Journal of Molecular Biology 306 5 1115 1126 doi 10 1006 jmbi 2001 4456 PMID 11237621 Duplay P Bedouelle H Fowler A Zabin I Saurin W Hofnung M August 1984 Sequences of the malE gene and of its product the maltose binding protein of Escherichia coli K12 The Journal of Biological Chemistry 259 16 10606 13 doi 10 1016 S0021 9258 18 91005 7 PMID 6088507 Spurlino JC Lu GY Quiocho FA March 1991 The 2 3 A resolution structure of the maltose or maltodextrin binding protein a primary receptor of bacterial active transport and chemotaxis The Journal of Biological Chemistry 266 8 5202 19 doi 10 2210 pdb1mbp pdb PMID 2002054 Sharff AJ Rodseth LE Spurlino JC Quiocho FA November 1992 Crystallographic evidence of a large ligand induced hinge twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis Biochemistry 31 44 10657 63 doi 10 1021 bi00159a003 PMID 1420181 Ferenci T Randall LL October 1979 Precursor maltose binding protein is active in binding substrate The Journal of Biological Chemistry 254 20 9979 81 doi 10 1016 S0021 9258 19 86659 0 PMID 385604 Park S Liu G Topping TB Cover WH Randall LL February 1988 Modulation of folding pathways of exported proteins by the leader sequence Science 239 4843 1033 5 Bibcode 1988Sci 239 1033P doi 10 1126 science 3278378 PMID 3278378 Beena K Udgaonkar JB Varadarajan R March 2004 Effect of signal peptide on the stability and folding kinetics of maltose binding protein Biochemistry 43 12 3608 19 doi 10 1021 bi0360509 PMID 15035631 Chun SY Strobel S Bassford P Randall LL October 1993 Folding of maltose binding protein Evidence for the identity of the rate determining step in vivo and in vitro The Journal of Biological Chemistry 268 28 20855 62 doi 10 1016 S0021 9258 19 36864 4 PMID 8407916 Kellermann O Szmelcman S August 1974 Active transport of maltose in Escherichia coli K12 Involvement of a periplasmic maltose binding protein European Journal of Biochemistry 47 1 139 49 doi 10 1111 j 1432 1033 1974 tb03677 x PMID 4215651 Randall LL Hardy SJ September 1986 Correlation of competence for export with lack of tertiary structure of the mature species a study in vivo of maltose binding protein in E coli Cell 46 6 921 8 doi 10 1016 0092 8674 86 90074 7 PMID 3530497 S2CID 28503725 Bedouelle H Bassford PJ Fowler AV Zabin I Beckwith J Hofnung M May 1980 Mutations which alter the function of the signal sequence of the maltose binding protein of Escherichia coli Nature 285 5760 78 81 Bibcode 1980Natur 285 78B doi 10 1038 285078a0 PMID 6990274 S2CID 4253747 Bedouelle H Hofnung M 1981 Functional implications of secondary structure analysis of wild type and mutant bacterial signal peptides Progress in Clinical and Biological Research 63 399 403 PMID 7312870 Chou YT Gierasch LM September 2005 The conformation of a signal peptide bound by Escherichia coli preprotein translocase SecA The Journal of Biological Chemistry 280 38 32753 60 doi 10 1074 jbc M507532200 PMID 16046390 Gelis I Bonvin AM Keramisanou D Koukaki M Gouridis G Karamanou S Economou A Kalodimos CG November 2007 Structural basis for signal sequence recognition by the translocase motor SecA as determined by NMR Cell 131 4 756 69 doi 10 1016 j cell 2007 09 039 PMC 2170882 PMID 18022369 Boos W Shuman H March 1998 Maltose maltodextrin system of Escherichia coli transport metabolism and regulation Microbiology and Molecular Biology Reviews 62 1 204 29 doi 10 1128 MMBR 62 1 204 229 1998 PMC 98911 PMID 9529892 a b Bedouelle H Schmeissner U Hofnung M Rosenberg M November 1982 Promoters of the malEFG and malK lamB operons in Escherichia coli K12 Journal of Molecular Biology 161 4 519 31 doi 10 1016 0022 2836 82 90405 3 PMID 6185687 Bedouelle H November 1983 Mutations in the promoter regions of the malEFG and malK lamB operons of Escherichia coli K12 Journal of Molecular Biology 170 4 861 82 doi 10 1016 s0022 2836 83 80192 2 PMID 6417341 Richet E October 2000 Synergistic transcription activation a dual role for CRP in the activation of an Escherichia coli promoter depending on MalT and CRP The EMBO Journal 19 19 5222 32 doi 10 1093 emboj 19 19 5222 PMC 302108 PMID 11013224 Richet E Raibaud O March 1989 MalT the regulatory protein of the Escherichia coli maltose system is an ATP dependent transcriptional activator The EMBO Journal 8 3 981 7 doi 10 1002 j 1460 2075 1989 tb03461 x PMC 400900 PMID 2524384 Schreiber V Richet E November 1999 Self association of the Escherichia coli transcription activator MalT in the presence of maltotriose and ATP The Journal of Biological Chemistry 274 47 33220 6 doi 10 1074 jbc 274 47 33220 PMID 10559195 Duplay P Bedouelle H Szmelcman S Hofnung M 1985 Linker mutagenesis in the gene encoding the periplasmic maltose binding protein of E coli Biochimie 67 7 8 849 51 doi 10 1016 s0300 9084 85 80178 4 PMID 3002495 Duplay P Szmelcman S Bedouelle H Hofnung M April 1987 Silent and functional changes in the periplasmic maltose binding protein of Escherichia coli K12 I Transport of maltose Journal of Molecular Biology 194 4 663 73 doi 10 1016 0022 2836 87 90243 9 PMID 2821264 Coeffier E Clement JM Cussac V Khodaei Boorane N Jehanno M Rojas M Dridi A Latour M El Habib R Barre Sinoussi F Hofnung M Leclerc C November 2000 Antigenicity and immunogenicity of the HIV 1 gp41 epitope ELDKWA inserted into permissive sites of the MalE protein Vaccine 19 7 8 684 93 doi 10 1016 s0264 410x 00 00267 x PMID 11115689 a b c Bedouelle H Duplay P February 1988 Production in Escherichia coli and one step purification of bifunctional hybrid proteins which bind maltose Export of the Klenow polymerase into the periplasmic space European Journal of Biochemistry 171 3 541 9 doi 10 1111 j 1432 1033 1988 tb13823 x PMID 3278900 Rondard P Bregegere F Lecroisey A Delepierre M Bedouelle H July 1997 Conformational and functional properties of an undecapeptide epitope fused with the C terminal end of the maltose binding protein Biochemistry 36 29 8954 61 CiteSeerX 10 1 1 599 2650 doi 10 1021 bi962508d PMID 9220983 di Guan C Li P Riggs PD Inouye H July 1988 Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose binding protein Gene 67 1 21 30 doi 10 1016 0378 1119 88 90004 2 PMID 2843437 Bregegere F Schwartz J Bedouelle H February 1994 Bifunctional hybrids between the variable domains of an immunoglobulin and the maltose binding protein of Escherichia coli production purification and antigen binding Protein Engineering 7 2 271 80 PMID 8170930 Malik A June 2016 Protein fusion tags for efficient expression and purification of recombinant proteins in the periplasmic space of E coli 3 Biotech 6 1 44 doi 10 1007 s13205 016 0397 7 PMC 4742420 PMID 28330113 Blondel A Bedouelle H October 1990 Export and purification of a cytoplasmic dimeric protein by fusion to the maltose binding protein of Escherichia coli European Journal of Biochemistry 193 2 325 30 doi 10 1111 j 1432 1033 1990 tb19341 x PMID 2226455 Kapust RB Waugh DS August 1999 Escherichia coli maltose binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused Protein Science 8 8 1668 74 doi 10 1110 ps 8 8 1668 PMC 2144417 PMID 10452611 Waugh DS March 2016 Crystal structures of MBP fusion proteins Protein Science 25 3 559 71 doi 10 1002 pro 2863 PMC 4815407 PMID 26682969 External links editN Terminal Fusion of Target Protein to Maltose Binding Protein at Michigan Technological University maltose binding protein at the U S National Library of Medicine Medical Subject Headings MeSH Generic protocol for the expression and purification of recombinant proteins in Escherichia coli using a combinatorial His6 maltose binding protein fusion tag Retrieved from https en wikipedia org w index php title Maltose binding protein amp oldid 1184038225, wikipedia, wiki, book, books, library,

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