malE

Summary

Gene Symbol: malE
Description: maltose transporter subunit
Alias: ECK4026, JW3994, malJ
Species: Escherichia coli str. K-12 substr. MG1655
Products:     malE

Top Publications

  1. Feilmeier B, Iseminger G, Schroeder D, Webber H, Phillips G. Green fluorescent protein functions as a reporter for protein localization in Escherichia coli. J Bacteriol. 2000;182:4068-76 pubmed
    ..GFP) as a reporter for protein localization in Escherichia coli was explored by creating gene fusions between malE (encoding maltose-binding protein [MBP]) and a variant of gfp optimized for fluorescence in bacteria (GFPuv)...
  2. Saul F, Mourez M, Vulliez Le Normand B, Sassoon N, Bentley G, Betton J. Crystal structure of a defective folding protein. Protein Sci. 2003;12:577-85 pubmed
    Maltose-binding protein (MBP or MalE) of Escherichia coli is the periplasmic receptor of the maltose transport system...
  3. Shuman H. Active transport of maltose in Escherichia coli K12. Role of the periplasmic maltose-binding protein and evidence for a substrate recognition site in the cytoplasmic membrane. J Biol Chem. 1982;257:5455-61 pubmed
    ..A model for the operation of the transport system is presented. In this model, the substrate recognition site in the cytoplasmic membrane is exposed to alternate sides of the membrane...
  4. Hunke S, Betton J. Temperature effect on inclusion body formation and stress response in the periplasm of Escherichia coli. Mol Microbiol. 2003;50:1579-89 pubmed
    ..Finally, expression of highly destabilized MalE variants that do not aggregate in the periplasm also induces the Cpx pathway, indicating that inclusion body ..
  5. Bedouelle H, Bassford P, Fowler A, Zabin I, Beckwith J, Hofnung M. Mutations which alter the function of the signal sequence of the maltose binding protein of Escherichia coli. Nature. 1980;285:78-81 pubmed
    ..In most cases, the change of a single hydrophobic or uncharged amino acid to a charged amino acid within the signal sequence is sufficient to block the secretion process...
  6. Betton J, Hofnung M. Folding of a mutant maltose-binding protein of Escherichia coli which forms inclusion bodies. J Biol Chem. 1996;271:8046-52 pubmed
    The maltose-binding protein (MalE) of Escherichia coli is the periplasmic component of the transport system for malto-oligosaccharides...
  7. Betton J, Boscus D, Missiakas D, Raina S, Hofnung M. Probing the structural role of an alpha beta loop of maltose-binding protein by mutagenesis: heat-shock induction by loop variants of the maltose-binding protein that form periplasmic inclusion bodies. J Mol Biol. 1996;262:140-50 pubmed
    ..the structural role of this surface loop, we generated a library in which the corresponding codons 32 and 33 of malE were mutagenized...
  8. Duplay P, Szmelcman S, Bedouelle H, Hofnung M. Silent and functional changes in the periplasmic maltose-binding protein of Escherichia coli K12. I. Transport of maltose. J Mol Biol. 1987;194:663-73 pubmed
    The malE gene encodes the periplasmic maltose-binding protein (MBP)...
  9. Boos W, Shuman H. Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation. Microbiol Mol Biol Rev. 1998;62:204-29 pubmed

More Information

Publications99

  1. Betton J, Sassoon N, Hofnung M, Laurent M. Degradation versus aggregation of misfolded maltose-binding protein in the periplasm of Escherichia coli. J Biol Chem. 1998;273:8897-902 pubmed
    ..A kinetic competition between folding, aggregation, and degradation is proposed as a general model for the biogenesis of periplasmic proteins...
  2. Spurlino J, Lu G, Quiocho F. The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J Biol Chem. 1991;266:5202-19 pubmed
    ..abstract truncated at 250 words)..
  3. Merino G, Shuman H. Truncation of MalF results in lactose transport via the maltose transport system of Escherichia coli. J Biol Chem. 1998;273:2435-44 pubmed
    ..The mutant requires functional MalK-ATPase activity and hydrolyzes ATP constitutively. It also requires MalG. The data suggest that in this mutant the MalG protein is capable of forming a low affinity transport path for substrate...
  4. Sung K, Song H. Direct recognition of the C-terminal polylysine residues of nonstop protein by Ltn1, an E3 ubiquitin ligase. Biochem Biophys Res Commun. 2014;453:642-7 pubmed publisher
    ..This biochemical characterization of Ltn1 expands our knowledge regarding the fundamental process that removes aberrant nascent polypeptides in eukaryotes. ..
  5. Keller R, Hunke S. Misfolded maltose binding protein MalE219 induces the CpxRA envelope stress response by stimulating phosphoryl transfer from CpxA to CpxR. Res Microbiol. 2009;160:396-400 pubmed publisher
    ..Consequently, we suggest that this direct interaction is a new mechanism enabling the Cpx pathway to sense misfolded proteins. ..
  6. Colonna B, Hofnung M. rho Mutations restore lamB expression in E. coli K12 strains with an inactive malB region. Mol Gen Genet. 1981;184:479-83 pubmed
    ..Experiments with Mu insertions in gene malK suggest that in the (-) orientation a Mu promoter is also able to allow lamB expression in a rho background. ..
  7. Dassa E, Lambert P. Activity of protein MalE (maltose-binding protein) fused to cytoplasmic and periplasmic regions of an Escherichia coli inner membrane protein. Res Microbiol. 1997;148:389-95 pubmed
    We analysed the properties of mature MBP (maltose-binding protein or MalE protein) fused to an integral cytoplasmic membrane protein of Escherichia coli...
  8. Polissi A, De Laurentis W, Zangrossi S, Briani F, Longhi V, Pesole G, et al. Changes in Escherichia coli transcriptome during acclimatization at low temperature. Res Microbiol. 2003;154:573-80 pubmed
    ..Interestingly, we found that PNPase both negatively and positively modulated the transcript abundance of some of these genes, thus suggesting a complex role of PNPase in controlling cold adaptation. ..
  9. Silhavy T, Brickman E, Bassford P, Casadaban M, Shuman H, Schwartz V, et al. Structure of the malB region in Escherichia coli K12. II. Genetic map of the malE,F,G operon. Mol Gen Genet. 1979;174:249-59 pubmed
    ..a strain containing a malK-lacZ fusion, a series of lambda plaque-forming phages which carry varying amounts of the malE,F operon have been isolated. We have used these phages to construct a deletion map of the malE,F operon...
  10. Meyer D, Schneider Fresenius C, Horlacher R, Peist R, Boos W. Molecular characterization of glucokinase from Escherichia coli K-12. J Bacteriol. 1997;179:1298-306 pubmed
    ..This demonstrates that free internal glucose plays an essential role in the formation of the endogenous inducer of the maltose system. ..
  11. Xu Y, Zheng Y, Fan J, Yang D. A new strategy for structure determination of large proteins in solution without deuteration. Nat Methods. 2006;3:931-7 pubmed
    ..The strategy extends the size limit for structure determination by NMR spectroscopy to 42 kDa for monomeric proteins and to 65 kDa for differentially labeled multimeric proteins without the need for deuteration or selective labeling. ..
  12. Steinke A, Grau S, Davidson A, Hofmann E, Ehrmann M. Characterization of transmembrane segments 3, 4, and 5 of MalF by mutational analysis. J Bacteriol. 2001;183:375-81 pubmed
    ..The phenotypes and locations of the mutations are consistent with a previously postulated structural model of MalF...
  13. Hall J, Davidson A, Nikaido H. Preparation and reconstitution of membrane-associated maltose transporter complex of Escherichia coli. Methods Enzymol. 1998;292:20-9 pubmed
  14. Mourez M, Jehanno M, Schneider E, Dassa E. In vitro interaction between components of the inner membrane complex of the maltose ABC transporter of Escherichia coli: modulation by ATP. Mol Microbiol. 1998;30:353-63 pubmed
  15. Chapon C. Role of the catabolite activator protein in the maltose regulon of Escherichia coli. J Bacteriol. 1982;150:722-9 pubmed
    ..On the other hand, it controls the other two operons more stringently, both by regulating malT expression and by a more direct action, probably exerted in the promoters of these operons. ..
  16. Gardina P, Bormans A, Hawkins M, Meeker J, Manson M. Maltose-binding protein interacts simultaneously and asymmetrically with both subunits of the Tar chemoreceptor. Mol Microbiol. 1997;23:1181-91 pubmed
  17. Prajapati R, Indu S, Varadarajan R. Identification and thermodynamic characterization of molten globule states of periplasmic binding proteins. Biochemistry. 2007;46:10339-52 pubmed
    ..The ability of these sequentially unrelated proteins to form highly ordered molten globules may be related to their large size as well as an intrinsic property of periplasmic binding protein folds. ..
  18. Srinivasan U, Iyer G, Przybycien T, Samsonoff W, Bell J. Crystine: fibrous biomolecular material from protein crystals cross-linked in a specific geometry. Protein Eng. 2002;15:895-902 pubmed
    ..Crystine fibers are a new type of biomolecular material with potential applications wherever the use of proteins in a fibrous form is desirable, for example, the incorporation of enzymes into cloth or filtration material. ..
  19. Joly N, BOHM A, Boos W, Richet E. MalK, the ATP-binding cassette component of the Escherichia coli maltodextrin transporter, inhibits the transcriptional activator malt by antagonizing inducer binding. J Biol Chem. 2004;279:33123-30 pubmed
    ..These results offer new insights into the mechanism by which gene regulation can be accomplished by the ATPase component of a bacterial ATP-binding cassette-type importer...
  20. Hor L, Shuman H. Genetic analysis of periplasmic binding protein dependent transport in Escherichia coli. Each lobe of maltose-binding protein interacts with a different subunit of the MalFGK2 membrane transport complex. J Mol Biol. 1993;233:659-70 pubmed
    ..In the other study, dominant mutations in malE (the structural gene of MBP) were isolated; one of these altered the same tyrosine residue (210) to cysteine...
  21. Diestra E, Fontana J, Guichard P, Marco S, Risco C. Visualization of proteins in intact cells with a clonable tag for electron microscopy. J Struct Biol. 2009;165:157-68 pubmed publisher
    ..The electron-dense tag was easily visualized by electron tomography and in frozen-hydrated cells. ..
  22. Duplay P, Bedouelle H, Fowler A, Zabin I, Saurin W, Hofnung M. Sequences of the malE gene and of its product, the maltose-binding protein of Escherichia coli K12. J Biol Chem. 1984;259:10606-13 pubmed
    The sequences of the malE gene and of its mature product, the maltose-binding protein, have been determined and are in good agreement...
  23. Hofnung M, Hatfield D, Schwartz M. malB region in Escherichia coli K-12: characterization of new mutations. J Bacteriol. 1974;117:40-7 pubmed
    ..the site for Mal(-)lambdas mutations (formerly called gene malB) in that region, into two adjacent genetic segments malJ and malK. malJ and malK are both involved in maltose permeation...
  24. Telmer P, Shilton B. Structural studies of an engineered zinc biosensor reveal an unanticipated mode of zinc binding. J Mol Biol. 2005;354:829-40 pubmed
    ..A comparison to the mechanism of maltose-induced domain rearrangement is discussed. ..
  25. Oldham M, Khare D, Quiocho F, Davidson A, Chen J. Crystal structure of a catalytic intermediate of the maltose transporter. Nature. 2007;450:515-21 pubmed
    ..These results provide direct evidence for a concerted mechanism of transport in which solute is transferred from the binding protein to the transmembrane subunits when the cassette dimer closes to hydrolyse ATP...
  26. Daus M, Grote M, Schneider E. The MalF P2 loop of the ATP-binding cassette transporter MalFGK2 from Escherichia coli and Salmonella enterica serovar typhimurium interacts with maltose binding protein (MalE) throughout the catalytic cycle. J Bacteriol. 2009;191:754-61 pubmed publisher
    ..MalFGK(2)) from Escherichia coli and Salmonella enterica serovar Typhimurium with maltose binding protein (MalE) by site-specific chemical cross-linking in the assembled transport complex...
  27. Ehrmann M, Beckwith J. Proper insertion of a complex membrane protein in the absence of its amino-terminal export signal. J Biol Chem. 1991;266:16530-3 pubmed
  28. Rubin S, Lee S, Ruiz E, Pines A, Wemmer D. Detection and characterization of xenon-binding sites in proteins by 129Xe NMR spectroscopy. J Mol Biol. 2002;322:425-40 pubmed
    ..Further applications of 129Xe NMR to biochemical assays, including the screening of proteins for xenon binding for crystallography are considered...
  29. Merino G, Shuman H. Unliganded maltose-binding protein triggers lactose transport in an Escherichia coli mutant with an alteration in the maltose transport system. J Bacteriol. 1997;179:7687-94 pubmed
    ..The requirement for MBP confirms that unliganded MBP interacts with the inner membrane MalFGK2 complex and that MBP plays a crucial role in triggering the transport process...
  30. Clausen T, Schlegel A, Peist R, Schneider E, Steegborn C, Chang Y, et al. X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression. EMBO J. 2000;19:831-42 pubmed
    ..Therefore, we propose that a direct protein-protein interaction with MalT, the central transcriptional activator of the maltose system, underlies MalY-dependent repression of the maltose system. ..
  31. Robichon C, Vidal Ingigliardi D, Pugsley A. Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli. J Biol Chem. 2005;280:974-83 pubmed
    ..Schmid, M. B., and Wu, H. C. (1993) J. Biol. Chem. 268, 16551-16556) was found to carry a mutation causing a single glutamate to lysine substitution at a highly conserved position in the last predicted periplasmic loop of the protein. ..
  32. Nikaido H. Maltose transport system of Escherichia coli: an ABC-type transporter. FEBS Lett. 1994;346:55-8 pubmed
    ..In addition, MBP performs a special function in the translocation of the larger ligands, maltodextrins, perhaps by aligning them for entry into the channel...
  33. Waugh D. The remarkable solubility-enhancing power of Escherichia coli maltose-binding protein. Postepy Biochem. 2016;62:377-382 pubmed
    ..W niniejszym krótkim artykule przegl?dowym przedstawiono aktualny stan wiedzy w zakresie zwi?kszania rozpuszczalno?ci innych bia?ek w wyniku fuzji z MBP, a jednocze?nie zachowywania prawid?owego fa?dowania tych bia?ek. ..
  34. Treptow N, Shuman H. Genetic evidence for substrate and periplasmic-binding-protein recognition by the MalF and MalG proteins, cytoplasmic membrane components of the Escherichia coli maltose transport system. J Bacteriol. 1985;163:654-60 pubmed
    ..These mutants were selected as Mal+ revertants of a strain which carries a deletion of the MBP structural gene, malE. In one class of these mutants, maltose is transported into the cell independently of MBP by the remaining ..
  35. Reidl J, Boos W. The malX malY operon of Escherichia coli encodes a novel enzyme II of the phosphotransferase system recognizing glucose and maltose and an enzyme abolishing the endogenous induction of the maltose system. J Bacteriol. 1991;173:4862-76 pubmed
    ..When constitutively expressed, malX can complement a ptsG ptsM double mutant for growth on glucose. Also, a delta malE malT(Con) strain that is unable to grow on maltose due to its maltose transport defect becomes Mal+ after ..
  36. Nallamsetty S, Waugh D. Mutations that alter the equilibrium between open and closed conformations of Escherichia coli maltose-binding protein impede its ability to enhance the solubility of passenger proteins. Biochem Biophys Res Commun. 2007;364:639-44 pubmed
    ..Our findings indicate that the solubility-enhancing activity of MBP is mediated by its open conformation and point to a likely role for the ligand-binding cleft in the mechanism of solubility enhancement. ..
  37. Ehrmann M, Boos W. Identification of endogenous inducers of the mal regulon in Escherichia coli. J Bacteriol. 1987;169:3539-45 pubmed
    ..coli linkage map. A Tn10 insertion in malI also resulted in the loss of constitutivity at low osmolarity and delayed the induction of the maltose regulon by exogenous inducers. ..
  38. Vidal Ingigliardi D, Raibaud O. Three adjacent binding sites for cAMP receptor protein are involved in the activation of the divergent malEp-malKp promoters. Proc Natl Acad Sci U S A. 1991;88:229-33 pubmed
    ..The participation of several adjacent bound CRP molecules in the activation of a promoter is an unprecedented observation and might involve molecular mechanisms quite different from those used in the other CRP-controlled promoters. ..
  39. Mannering D, Sharma S, Davidson A. Demonstration of conformational changes associated with activation of the maltose transport complex. J Biol Chem. 2001;276:12362-8 pubmed
  40. Telmer P, Shilton B. Insights into the conformational equilibria of maltose-binding protein by analysis of high affinity mutants. J Biol Chem. 2003;278:34555-67 pubmed
  41. Alvarez F, Orelle C, Huang Y, Bajaj R, Everly R, Klug C, et al. Full engagement of liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporter. Mol Microbiol. 2015;98:878-94 pubmed publisher
  42. McLaren R, Newbury S, Dance G, Causton H, Higgins C. mRNA degradation by processive 3'-5' exoribonucleases in vitro and the implications for prokaryotic mRNA decay in vivo. J Mol Biol. 1991;221:81-95 pubmed
    ..These data suggest that an additional factor, such as a stem-loop binding protein, is required for stabilization of mRNA by stem-loop structures in vivo. The implications for the regulation of mRNA stability are discussed. ..
  43. Davidson A, Nikaido H. Purification and characterization of the membrane-associated components of the maltose transport system from Escherichia coli. J Biol Chem. 1991;266:8946-51 pubmed
    ..Each complex contains two MalK, one MalF, and one MalG proteins, providing two putative sites for ATP hydrolysis. Chemical cross-linking detected specific interactions between MalF and MalG and between MalF and MalK...
  44. Decker K, Plumbridge J, Boos W. Negative transcriptional regulation of a positive regulator: the expression of malT, encoding the transcriptional activator of the maltose regulon of Escherichia coli, is negatively controlled by Mlc. Mol Microbiol. 1998;27:381-90 pubmed
    ..As Mlc also regulates another operon (manXYZ, see pages 369-379 of this issue), it may very well constitute a new global regulator of carbohydrate utilization...
  45. Kirkpatrick C, Maurer L, Oyelakin N, Yoncheva Y, Maurer R, Slonczewski J. Acetate and formate stress: opposite responses in the proteome of Escherichia coli. J Bacteriol. 2001;183:6466-77 pubmed
  46. Higgins C, McLaren R, Newbury S. Repetitive extragenic palindromic sequences, mRNA stability and gene expression: evolution by gene conversion? A review. Gene. 1988;72:3-14 pubmed
    ..Other possible functions for REP sequences are discussed. We propose that REP sequences may be a prokaryotic equivalent of 'selfish DNA' and that gene conversion may play a role in the evolution and maintenance of REP sequences. ..
  47. Dahl M, Manson M. Interspecific reconstitution of maltose transport and chemotaxis in Escherichia coli with maltose-binding protein from various enteric bacteria. J Bacteriol. 1985;164:1057-63 pubmed
    In Escherichia coli, the periplasmic maltose-binding protein (MBP), the product of the malE gene, is the primary recognition component of the transport system for maltose and maltodextrins...
  48. Han M, Lee J, Lee S, Yoo J. Proteome-level responses of Escherichia coli to long-chain fatty acids and use of fatty acid inducible promoter in protein production. J Biomed Biotechnol. 2008;2008:735101 pubmed publisher
    ..showing altered expression levels with oleic acid presence, 9 proteins including AldA, Cdd, FadA, FadB, FadL, MalE, RbsB, Udp, and YccU were newly synthesized...
  49. Tomkiewicz D, Nouwen N, Driessen A. Kinetics and energetics of the translocation of maltose binding protein folding mutants. J Mol Biol. 2008;377:83-90 pubmed publisher
    ..These data indicate that unfolding of the mature domain of preMBP is likely not a rate-determining step in translocation when the protein is targeted to the translocase via SecB. ..
  50. Jacso T, Grote M, Daus M, Schmieder P, Keller S, Schneider E, et al. Periplasmic loop P2 of the MalF subunit of the maltose ATP binding cassette transporter is sufficient to bind the maltose binding protein MalE. Biochemistry. 2009;48:2216-25 pubmed publisher
    ..experiments shows that the conformation of the two individual domains of MalF-P2 is preserved in the absence of MalE and resembles the conformation in the X-ray structure...
  51. Kainosho M, Torizawa T, Iwashita Y, Terauchi T, Mei Ono A, Güntert P. Optimal isotope labelling for NMR protein structure determinations. Nature. 2006;440:52-7 pubmed
    ..It thus makes a large class of proteins newly accessible to detailed solution structure determination. ..
  52. Randall L, Hardy S, Josefsson L. Precursors of three exported proteins in Escherichia coli. Proc Natl Acad Sci U S A. 1978;75:1209-12 pubmed
    ..In contrast to the above, when the intracellular protein elongation factor Tu is synthesized in vitro on free polysomes, it is not detectably larger than the authentic form. ..
  53. Mueller G, Choy W, Yang D, Forman Kay J, Venters R, Kay L. Global folds of proteins with low densities of NOEs using residual dipolar couplings: application to the 370-residue maltodextrin-binding protein. J Mol Biol. 2000;300:197-212 pubmed
    ..When applied to experimental data recorded on MBP the precision of the family of structures generated improves from 5.5 to 2.2 A, while the rmsd with respect to the X-ray structure (1dmb) is reduced from 5.1 to 3.3 A. ..
  54. Kossmann M, Wolff C, Manson M. Maltose chemoreceptor of Escherichia coli: interaction of maltose-binding protein and the tar signal transducer. J Bacteriol. 1988;170:4516-21 pubmed
    ..We previously isolated strains containing malE mutations that cause specific defects in the chemotactic function of MBP...
  55. Dahl M, Francoz E, Saurin W, Boos W, Manson M, Hofnung M. Comparison of sequences from the malB regions of Salmonella typhimurium and Enterobacter aerogenes with Escherichia coli K12: a potential new regulatory site in the interoperonic region. Mol Gen Genet. 1989;218:199-207 pubmed
    The malE and malK genes from Salmonella typhimurium, and the malEFG operon and a portion of malK from Enterobacter aerogenes were cloned and sequenced. Plasmid-borne malE genes from both species and the malF and malG genes from E...
  56. Wandersman C, Schwartz M, Ferenci T. Escherichia coli mutants impaired in maltodextrin transport. J Bacteriol. 1979;140:1-13 pubmed
    ..A second class of mutants were affected in malE, the structural gene of the periplasmic maltose binding protein...
  57. Raibaud O, Clement J, Hofnung M. Structure of the malB region in Escherichia coli K12. III. Correlation of the genetic map with the restriction map. Mol Gen Genet. 1979;174:261-7 pubmed
    ..This also allowed to localize the boundaries between malF and malE, malE and malK, mal K and lamB on the restriction map...
  58. Daus M, Grote M, Muller P, Doebber M, Herrmann A, Steinhoff H, et al. ATP-driven MalK dimer closure and reopening and conformational changes of the "EAA" motifs are crucial for function of the maltose ATP-binding cassette transporter (MalFGK2). J Biol Chem. 2007;282:22387-96 pubmed
    ..Substrate is delivered to the transporter in complex with periplasmic maltose-binding protein (MalE)...
  59. Dean D, Hor L, Shuman H, Nikaido H. Interaction between maltose-binding protein and the membrane-associated maltose transporter complex in Escherichia coli. Mol Microbiol. 1992;6:2033-40 pubmed
    ..When the wild-type malE+ allele, coding for MBP, was introduced into these MBP-independent mutants, they frequently lost their ability to ..
  60. Sharma S, Davis J, Ayvaz T, Traxler B, Davidson A. Functional reassembly of the Escherichia coli maltose transporter following purification of a MalF-MalG subassembly. J Bacteriol. 2005;187:2908-11 pubmed
    ..This MalF-MalG complex was competent for efficient reassembly of a functional MalFGK(2) maltose transporter complex both in detergent solution and in proteoliposomes...
  61. Mourez M, Skouloubris S, Betton J, Dassa E. Heat shock induction by a misassembled cytoplasmic membrane protein complex in Escherichia coli. Mol Microbiol. 1997;26:821-31 pubmed
    ..120 amino acids do not induce the phtrA promoter; (ii) the export to the periplasm of the L3 loop alone or fused to MalE induces the phtrA promoter...
  62. Manson M, Boos W, Bassford P, Rasmussen B. Dependence of maltose transport and chemotaxis on the amount of maltose-binding protein. J Biol Chem. 1985;260:9727-33 pubmed
    ..To determine how the amount of MBP affects transport and taxis, we utilized a series of malE signal-sequence mutations that interfere with export of MBP...
  63. Sharma S, Chakraborty K, Müller B, Astola N, Tang Y, Lamb D, et al. Monitoring protein conformation along the pathway of chaperonin-assisted folding. Cell. 2008;133:142-53 pubmed publisher
    ..Segmental chain release and compaction may be important in avoiding misfolding by proteins that fail to fold efficiently through spontaneous hydrophobic collapse. ..
  64. Kellermann O, Szmelcman S. Active transport of maltose in Escherichia coli K12. Involvement of a "periplasmic" maltose binding protein. Eur J Biochem. 1974;47:139-49 pubmed
  65. Raibaud O, Roa M, Braun Breton C, Schwartz M. Structure of the malB region in Escherichia coli K12. I. Genetic map of the malK-lamB operon. Mol Gen Genet. 1979;174:241-8 pubmed
  66. Manson M, Kossmann M. Mutations in tar suppress defects in maltose chemotaxis caused by specific malE mutations. J Bacteriol. 1986;165:34-40 pubmed
    Maltose-binding protein (MBP), which is encoded by the malE gene, is the maltose chemoreceptor of Escherichia coli, as well as an essential component of the maltose uptake system...
  67. Arié J, Miot M, Sassoon N, Betton J. Formation of active inclusion bodies in the periplasm of Escherichia coli. Mol Microbiol. 2006;62:427-37 pubmed
    ..we have analysed the cellular fates of exported proteins fused to either the wild-type maltose-binding protein (MalE) or the aggregation-prone variant MalE31...
  68. Panagiotidis C, Shuman H. Maltose transport in Escherichia coli: mutations that uncouple ATP hydrolysis from transport. Methods Enzymol. 1998;292:30-9 pubmed
  69. Guntas G, Mansell T, Kim J, Ostermeier M. Directed evolution of protein switches and their application to the creation of ligand-binding proteins. Proc Natl Acad Sci U S A. 2005;102:11224-9 pubmed
    ..The transplantation of these mutations into wild-type MBP converted MBP into a "sucrose-binding protein," illustrating the switches potential as a tool to rapidly identify ligand-binding proteins. ..
  70. Collier D, Bassford P. Mutations that improve export of maltose-binding protein in SecB- cells of Escherichia coli. J Bacteriol. 1989;171:4640-7 pubmed
    ..These results provide additional strong support for the proposed antifolding role of SecB in MBP export...
  71. Kulothungan S, Das M, Johnson M, Ganesh C, Varadarajan R. Effect of crowding agents, signal peptide, and chaperone SecB on the folding and aggregation of E. coli maltose binding protein. Langmuir. 2009;25:6637-48 pubmed publisher
    ..These experiments also demonstrate that signal peptide can greatly influence protein stability and aggregation propensity. ..
  72. Ehrle R, Pick C, Ulrich R, Hofmann E, Ehrmann M. Characterization of transmembrane domains 6, 7, and 8 of MalF by mutational analysis. J Bacteriol. 1996;178:2255-62 pubmed
    ..The majority of mutations in membrane-spanning segment 8 caused a Mal+ Dex- phenotype. Six Mal+ suppressor mutations isolated to two mutations in transmembrane domain 7 changed amino acid residues in membrane-spanning segment 6 or 8...
  73. Grote M, Polyhach Y, Jeschke G, Steinhoff H, Schneider E, Bordignon E. Transmembrane signaling in the maltose ABC transporter MalFGK2-E: periplasmic MalF-P2 loop communicates substrate availability to the ATP-bound MalK dimer. J Biol Chem. 2009;284:17521-6 pubmed publisher
    ..The EPR data revealed that the substrate-binding protein MalE is bound to the transporter throughout the transport cycle...
  74. Bechtluft P, van Leeuwen R, Tyreman M, Tomkiewicz D, Nouwen N, Tepper H, et al. Direct observation of chaperone-induced changes in a protein folding pathway. Science. 2007;318:1458-61 pubmed
    ..It appears that SecB only binds to the extended or molten globulelike structure and retains MBP in this latter state. Thus during MBP translocation, no energy is required to disrupt stable tertiary interactions. ..
  75. Zhang Y, Gardina P, Kuebler A, Kang H, Christopher J, Manson M. Model of maltose-binding protein/chemoreceptor complex supports intrasubunit signaling mechanism. Proc Natl Acad Sci U S A. 1999;96:939-44 pubmed
    ..Mutations were introduced into a plasmid-borne malE gene that encodes a mutant form of MBP in which two engineered Cys residues spontaneously generate a disulfide bond ..
  76. Treptow N, Shuman H. Allele-specific malE mutations that restore interactions between maltose-binding protein and the inner-membrane components of the maltose transport system. J Mol Biol. 1988;202:809-22 pubmed
    ..LamB, a periplasmic maltose-binding protein (MalE, MBP) and three inner-membrane proteins, MalF, MalG and MalK...
  77. Higgins C, Hiles I, Whalley K, Jamieson D. Nucleotide binding by membrane components of bacterial periplasmic binding protein-dependent transport systems. EMBO J. 1985;4:1033-9 pubmed
    ..The hisP, malK and oppD proteins are thus responsible for energy-coupling to their respective transport systems. ..
  78. Dattelbaum J, Looger L, Benson D, Sali K, Thompson R, Hellinga H. Analysis of allosteric signal transduction mechanisms in an engineered fluorescent maltose biosensor. Protein Sci. 2005;14:284-91 pubmed
    ..Taken together these results provide insights that can be used in future design cycles to construct fluorescent biosensors that optimize signaling by engineering specific hydrogen bonds between a fluorophore and protein. ..
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