secB

Summary

Gene Symbol: secB
Description: protein export chaperone
Alias: ECK3599, JW3584
Species: Escherichia coli str. K-12 substr. MG1655
Products:     secB

Top Publications

  1. Chen Y, Tai P, Sui S. The active ring-like structure of SecA revealed by electron crystallography: conformational change upon interaction with SecB. J Struct Biol. 2007;159:149-53 pubmed
    ..This pore structure is altered after transferring crystals to the SecB solution, indicating that the lipid-specific SecA structure has the SecB binding activity...
  2. Ureta A, Endres R, Wingreen N, Silhavy T. Kinetic analysis of the assembly of the outer membrane protein LamB in Escherichia coli mutants each lacking a secretion or targeting factor in a different cellular compartment. J Bacteriol. 2007;189:446-54 pubmed
    ..This kinetic analysis revealed that secB and secD mutants exhibit nearly identical defects in precursor translocation from the cytoplasm...
  3. Randall L, Crane J, Lilly A, Liu G, Mao C, Patel C, et al. Asymmetric binding between SecA and SecB two symmetric proteins: implications for function in export. J Mol Biol. 2005;348:479-89 pubmed
    b>SecB, a small tetrameric chaperone in Escherichia coli, facilitates export of precursor polypeptides from the cytoplasm to the periplasmic space. During this process, SecB displays two modes of binding...
  4. Dekker C, de Kruijff B, Gros P. Crystal structure of SecB from Escherichia coli. J Struct Biol. 2003;144:313-9 pubmed
    The chaperone SecB from Escherichia coli is primarily involved in passing precursor proteins into the Sec system via specific interactions with SecA. The crystal structure of SecB from E. coli has been solved to 2.35 A resolution...
  5. Fekkes P, van der Does C, Driessen A. The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation. EMBO J. 1997;16:6105-13 pubmed
    The chaperone SecB keeps precursor proteins in a translocation-competent state and targets them to SecA at the translocation sites in the cytoplasmic membrane of Escherichia coli. SecA is thought to recognize SecB via its carboxy-terminus...
  6. Ernst F, Hoffschulte H, Thome Kromer B, Swidersky U, Werner P, Muller M. Precursor-specific requirements for SecA, SecB, and delta muH+ during protein export of Escherichia coli. J Biol Chem. 1994;269:12840-5 pubmed
    ..protein Skp of Escherichia coli and demonstrate a precursor-specific dependence on the export factors SecA, SecB, and the proton-motive force (delta mu H+)...
  7. Randall L. Peptide binding by chaperone SecB: implications for recognition of nonnative structure. Science. 1992;257:241-5 pubmed
    The molecular basis for recognition of nonnative proteins by the molecular chaperone SecB was investigated with an in vitro assay based on the protection of SecB from proteolysis when a ligand is bound...
  8. Wild J, Altman E, Yura T, Gross C. DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli. Genes Dev. 1992;6:1165-72 pubmed
    ..This function is carried out by a group of proteins called chaperones. SecB is the major chaperone that interacts with precursor proteins before their secretion...
  9. Koch H, Muller M. Dissecting the translocase and integrase functions of the Escherichia coli SecYEG translocon. J Cell Biol. 2000;150:689-94 pubmed
    Recent evidence suggests that in Escherichia coli, SecA/SecB and signal recognition particle (SRP) are constituents of two different pathways targeting secretory and inner membrane proteins to the SecYEG translocon of the plasma membrane...

More Information

Publications79

  1. Beall B, Lutkenhaus J. Sequence analysis, transcriptional organization, and insertional mutagenesis of the envA gene of Escherichia coli. J Bacteriol. 1987;169:5408-15 pubmed
    ..Transcription of envA and the upstream fts genes terminated at this terminator and was probably uncoupled from the downstream genes, including secA. Gene disruption experiments indicated that the envA gene was an essential gene. ..
  2. Volkert T, Baleja J, Kumamoto C. A highly mobile C-terminal tail of the Escherichia coli protein export chaperone SecB. Biochem Biophys Res Commun. 1999;264:949-54 pubmed
    The Escherichia coli export chaperone SecB binds nascent precursors of certain periplasmic and outer membrane proteins and prevents them from folding or aggregating in the cytoplasm...
  3. Chen H, Kim J, Kendall D. Competition between functional signal peptides demonstrates variation in affinity for the secretion pathway. J Bacteriol. 1996;178:6658-64 pubmed
    ..consequences: preproteins with the more hydrophobic signals could dominate one pathway, leaving those with only slightly less hydrophobic signals to require additional factors such as chaperonins, SecB, and other binding proteins.
  4. Suo Y, Hardy S, Randall L. The basis of asymmetry in the SecA:SecB complex. J Mol Biol. 2015;427:887-900 pubmed publisher
    During export in Escherichia coli, SecB, a homotetramer structurally organized as a dimer of dimers, forms a complex with two protomers of SecA, which is the ATPase that provides energy to transfer a precursor polypeptide through the ..
  5. Dekker C, De Kruijff B, de Korte Kool G, Kroon J, Gros P. Crystals of acetylated SecB diffract to 2.3-A resolution. J Struct Biol. 1999;128:237-42 pubmed
    The molecular chaperone SecB is part of the protein translocation pathway in Escherichia coli. SecB was purified from an overproducing strain and crystallized, resulting in crystals diffracting to 2.3-A resolution...
  6. Bieker K, Silhavy T. The genetics of protein secretion in E. coli. Trends Genet. 1990;6:329-34 pubmed
    ..The picture emerging provides a useful paradigm for similar pathways in other organisms. ..
  7. Muller J. Effects of pre-protein overexpression on SecB synthesis in Escherichia coli. FEMS Microbiol Lett. 1999;176:219-27 pubmed
    ..The export-dedicated chaperone SecB mediates targeting of a subset of pre-proteins...
  8. Witt S. Tethering creates unusual kinetics for ribosome-associated chaperones with nascent chains. Protein Pept Lett. 2009;16:631-4 pubmed
    ..Ribosome-bound chaperones bind nascent chains intramolecularly with rates as large as 10(4) s(-1) in order to keep chains unfolded. ..
  9. Trun N, Stader J, Lupas A, Kumamoto C, Silhavy T. Two cellular components, PrlA and SecB, that recognize different sequence determinants are required for efficient protein export. J Bacteriol. 1988;170:5928-30 pubmed
    We exploited the conditional-lethal phenotype of secB null mutations to demonstrate that SecB function was required for PrlA-mediated suppression of signal sequence mutations...
  10. Khokhlova O, Nesmeianova M. [Interaction of effect on secretion of alkaline phosphatase from E. coli by charge of the N-terminal part of the signal peptide and proteins SecB and SecA]. Mol Biol (Mosk). 2004;38:288-96 pubmed
    The cytoplasmic step of posttranslational secretion in Escherichia coli is catalyzed by export-specific chaperone SecB and translocational ATPase SecA...
  11. Collier D, Strobel S, Bassford P. SecB-independent export of Escherichia coli ribose-binding protein (RBP): some comparisons with export of maltose-binding protein (MBP) and studies with RBP-MBP hybrid proteins. J Bacteriol. 1990;172:6875-84 pubmed
    The efficient export of the Escherichia coli maltose-binding protein (MBP) is known to be SecB dependent, whereas ribose-binding protein (RBP) export is SecB independent...
  12. de Keyzer J, van der Sluis E, Spelbrink R, Nijstad N, de Kruijff B, Nouwen N, et al. Covalently dimerized SecA is functional in protein translocation. J Biol Chem. 2005;280:35255-60 pubmed
    ..Cross-linking reversibly disrupts the SecB binding site on SecA...
  13. Woodbury R, Topping T, Diamond D, Suciu D, Kumamoto C, Hardy S, et al. Complexes between protein export chaperone SecB and SecA. Evidence for separate sites on SecA providing binding energy and regulatory interactions. J Biol Chem. 2000;275:24191-8 pubmed
    ..or to the outer membrane of Escherichia coli some proteins are dependent on binding to the cytosolic chaperone SecB, which in turn is targeted to the membrane by specific interaction with SecA, a peripheral component of the ..
  14. Seoh H, Tai P. Catabolic repression of secB expression is positively controlled by cyclic AMP (cAMP) receptor protein-cAMP complexes at the transcriptional level. J Bacteriol. 1999;181:1892-9 pubmed
    b>SecB, a protein export-specific chaperone, enhances the export of a subset of proteins across cytoplasmic membranes of Escherichia coli...
  15. Lilly A, Crane J, Randall L. Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands. Protein Sci. 2009;18:1860-8 pubmed publisher
    b>SecB, a remarkable chaperone involved in protein export, binds diverse ligands rapidly with high affinity and low specificity...
  16. Vrielink A, Beamer L, Le T, Eisenberg D. Crystallization of the chaperone protein SecB. Protein Sci. 1995;4:1651-3 pubmed
    The secretory protein SecB found in Escherichia coli is a molecular chaperone that binds to precursor forms of a number of proteins targeted for export to the periplasmic space...
  17. 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
    ..With the use of optical tweezers and all-atom molecular dynamics simulations, we studied the effect of chaperone SecB on the folding and unfolding pathways of maltose binding protein (MBP) at the single-molecule level...
  18. Crane J, Suo Y, Lilly A, Mao C, Hubbell W, Randall L. Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labeling. J Mol Biol. 2006;363:63-74 pubmed
    ..Capture of the precursor polypeptides before they fold is achieved by the promiscuous binding to the chaperone SecB. SecB delivers its ligand to export sites through its specific binding to SecA, a peripheral component of the ..
  19. Patel C, Smith V, Randall L. Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export. Protein Sci. 2006;15:1379-86 pubmed
    ..b>SecB, a small cytosolic chaperone, captures the precursor polypeptides before they fold and delivers them to the ..
  20. Randall L, Topping T, Suciu D, Hardy S. Calorimetric analyses of the interaction between SecB and its ligands. Protein Sci. 1998;7:1195-200 pubmed
    b>SecB is a chaperone in Escherichia coli dedicated to export of proteins from the cytoplasm to the periplasm and outer membrane...
  21. Panse V, Swaminathan C, Aloor J, Surolia A, Varadarajan R. Unfolding thermodynamics of the tetrameric chaperone, SecB. Biochemistry. 2000;39:2362-9 pubmed
    b>SecB is a cytosolic tetrameric chaperone in Escherichia coli, which maintains polypeptides, destined for export in a translocation competent state...
  22. Zhou J, Xu Z. The structural view of bacterial translocation-specific chaperone SecB: implications for function. Mol Microbiol. 2005;58:349-57 pubmed
    b>SecB is a molecular chaperone that functions in bacterial post-translational protein translocation pathway...
  23. Ullers R, Ang D, Schwager F, Georgopoulos C, Genevaux P. Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli. Proc Natl Acad Sci U S A. 2007;104:3101-6 pubmed
    ..In Escherichia coli, the chaperones SecB, Trigger Factor (TF), and DnaK are key players in this process...
  24. Krishnan B, Kulothungan S, Patra A, Udgaonkar J, Varadarajan R. SecB-mediated protein export need not occur via kinetic partitioning. J Mol Biol. 2009;385:1243-56 pubmed publisher
    In Escherichia coli, the cytosolic chaperone SecB is responsible for the selective entry of a subset of precursor proteins into the Sec pathway...
  25. Watanabe M, Blobel G. High-affinity binding of Escherichia coli SecB to the signal sequence region of a presecretory protein. Proc Natl Acad Sci U S A. 1995;92:10133-6 pubmed
    The Escherichia coli cytosolic homotetrameric protein SecB is known to be involved in protein export across the plasma membrane...
  26. Den Blaauwen T, Terpetschnig E, Lakowicz J, Driessen A. Interaction of SecB with soluble SecA. FEBS Lett. 1997;416:35-8 pubmed
    The preprotein binding molecular chaperone SecB functions by preventing the premature folding of the preprotein in the cytosol, and targeting it to the peripheral subunit SecA of the translocase at the cytoplasmic membrane...
  27. Knoblauch N, Rudiger S, Schönfeld H, Driessen A, Schneider Mergener J, Bukau B. Substrate specificity of the SecB chaperone. J Biol Chem. 1999;274:34219-25 pubmed
    The bacterial chaperone SecB assists translocation of proteins across the inner membrane. The mechanism by which it differentiates between secretory and cytosolic proteins is poorly understood...
  28. Gatsos X, Perry A, Anwari K, Dolezal P, Wolynec P, Likic V, et al. Protein secretion and outer membrane assembly in Alphaproteobacteria. FEMS Microbiol Rev. 2008;32:995-1009 pubmed publisher
  29. Watanabe M, Blobel G. Cytosolic factor purified from Escherichia coli is necessary and sufficient for the export of a preprotein and is a homotetramer of SecB. Proc Natl Acad Sci U S A. 1989;86:2728-32 pubmed
    ..Amino-terminal sequence analysis revealed that it is identical to the secB gene product...
  30. Kim J, Lee Y, Kim C, Park C. Involvement of SecB, a chaperone, in the export of ribose-binding protein. J Bacteriol. 1992;174:5219-27 pubmed
    ..b>SecB protein, a chaperone known to mediate the export of some periplasmic and outer membrane proteins, was previously ..
  31. Panse V, Swaminathan C, Surolia A, Varadarajan R. Thermodynamics of substrate binding to the chaperone SecB. Biochemistry. 2000;39:2420-7 pubmed
    The thermodynamics of binding of unfolded polypeptides to the chaperone SecB was investigated in vitro by isothermal titration calorimetry and fluorescence spectroscopy...
  32. Kumamoto C, Nault A. Characterization of the Escherichia coli protein-export gene secB. Gene. 1989;75:167-75 pubmed
    The Escherichia coli secB gene product is required for normal export of envelope proteins out of the cell cytoplasm. In this report, we present the identification and nucleotide sequence of the secB coding sequence...
  33. Estevenon A, Lemonnier M, Rouquette C, Lane D. Genetic basis of the MbrC "ploidy" phenotype in Escherichia coli. Mol Gen Genet. 1997;256:291-7 pubmed
    ..This mutation causes a two-fold increase in the concentration of secE-nusG mRNA. ..
  34. Topping T, Randall L. Determination of the binding frame within a physiological ligand for the chaperone SecB. Protein Sci. 1994;3:730-6 pubmed
    ..the molecular mechanism of such remarkable binding, we have characterized complexes between the bacterial chaperone SecB and a series of ligands related to maltose-binding protein...
  35. Dawid A, Cayrol B, Isambert H. RNA synthetic biology inspired from bacteria: construction of transcription attenuators under antisense regulation. Phys Biol. 2009;6:025007 pubmed publisher
    ..Overall, this suggests that direct coupling among synthesis, folding and regulation of RNAs may have enabled the early emergence of autonomous RNA-based regulation networks in absence of both DNA and protein partners. ..
  36. Miller A, Wang L, Kendall D. SecB modulates the nucleotide-bound state of SecA and stimulates ATPase activity. Biochemistry. 2002;41:5325-32 pubmed
    In Escherichia coli, the formation of SecA-SecB complexes has a direct effect on SecA ATPase activity...
  37. Fekkes P, de Wit J, Boorsma A, Friesen R, Driessen A. Zinc stabilizes the SecB binding site of SecA. Biochemistry. 1999;38:5111-6 pubmed
    The molecular chaperone SecB targets preproteins to SecA at the translocation sites in the cytoplasmic membrane of Escherichia coli...
  38. Randall L, Crane J, Liu G, Hardy S. Sites of interaction between SecA and the chaperone SecB, two proteins involved in export. Protein Sci. 2004;13:1124-33 pubmed
    b>SecB, a small tetrameric cytosolic chaperone in Escherichia coli, facilitates the export of precursor poly-peptides by maintaining them in a nonnative conformation and passing them to SecA, which is a peripheral member of the membrane-..
  39. Kumamoto C. Escherichia coli SecB protein associates with exported protein precursors in vivo. Proc Natl Acad Sci U S A. 1989;86:5320-4 pubmed
    The product of the Escherichia coli secB gene is required for efficient export of proteins across the cytoplasmic membrane...
  40. Kim J, Kendall D. Identification of a sequence motif that confers SecB dependence on a SecB-independent secretory protein in vivo. J Bacteriol. 1998;180:1396-401 pubmed
    b>SecB is a cytosolic chaperone which facilitates the transport of a subset of proteins, including membrane proteins such as PhoE and LamB and some periplasmic proteins such as maltose-binding protein, in Escherichia coli...
  41. Panse V, Udgaonkar J, Varadarajan R. SecB binds only to a late native-like intermediate in the folding pathway of barstar and not to the unfolded state. Biochemistry. 1998;37:14477-83 pubmed
    b>SecB is a cytosolic, tetrameric chaperone of Escherichia coli which maintains precursor proteins in a translocation competent state...
  42. Powers E, Randall L. Export of periplasmic galactose-binding protein in Escherichia coli depends on the chaperone SecB. J Bacteriol. 1995;177:1906-7 pubmed
    The efficient export of galactose-binding protein to the periplasm of Escherichia coli is shown to be dependent on the presence of the cytosolic chaperone SecB.
  43. Panse V, Vogel P, Trommer W, Varadarajan R. A thermodynamic coupling mechanism for the disaggregation of a model peptide substrate by chaperone secB. J Biol Chem. 2000;275:18698-703 pubmed
    ..b>SecB is a cytosolic chaperone, which forms part of the precursor protein translocation machinery in Escherichia coli...
  44. de Keyzer J, van der Does C, Driessen A. The bacterial translocase: a dynamic protein channel complex. Cell Mol Life Sci. 2003;60:2034-52 pubmed
    ..Many secretory proteins utilize the molecular chaperone SecB for targeting and stabilization of the unfolded state prior to translocation, while most nascent inner membrane ..
  45. Kimsey H, Dagarag M, Kumamoto C. Diverse effects of mutation on the activity of the Escherichia coli export chaperone SecB. J Biol Chem. 1995;270:22831-5 pubmed
    The Escherichia coli SecB protein binds newly synthesized precursor maltose-binding protein (preMBP) and promotes its rapid export from the cytoplasm...
  46. Tang Y, Pan X, Tai P, Sui S. The structure of SecB/OmpA as visualized by electron microscopy: The mature region of the precursor protein binds asymmetrically to SecB. Biochem Biophys Res Commun. 2010;393:698-702 pubmed publisher
    b>SecB, a molecular chaperone in Escherichia coli, binds a subset of precursor proteins that are exported across the plasma membrane via the Sec pathway...
  47. Mao C, Hardy S, Randall L. Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by SecB requires two protomers of SecA. J Bacteriol. 2009;191:978-84 pubmed publisher
    ..We showed previously that when SecA receives the precursor from SecB, the ternary complex is fully active only when two protomers of SecA are bound...
  48. Shimohata N, Akiyama Y, Ito K. Peculiar properties of DsbA in its export across the Escherichia coli cytoplasmic membrane. J Bacteriol. 2005;187:3997-4004 pubmed
    ..DsbA export depended on the SecY translocon, the SecA ATPase, and Ffh (signal recognition particle), but not on SecB. SecY mutations, such as secY39 and secY205, that severely impair translocation of a number of secretory substrates ..
  49. Randall L, Topping T, Smith V, Diamond D, Hardy S. SecB: a chaperone from Escherichia coli. Methods Enzymol. 1998;290:444-59 pubmed
  50. Linde D, Marischen L, Müller J. Characterisation of preYvaY export reveals differences in the substrate specificities of Bacillus subtilis and Escherichia coli leader peptidases. FEMS Microbiol Lett. 2003;227:149-56 pubmed
    ..coli LepB and the B. subtilis Sip proteins provide the bottleneck for export of YvaY in E. coli. Significant slower processing of preYvaY in absence of SecB indicated that SecB mediates targeting of the B. subtilis precursor.
  51. Kumamoto C, Beckwith J. Evidence for specificity at an early step in protein export in Escherichia coli. J Bacteriol. 1985;163:267-74 pubmed
    We previously described mutations in a gene, secB, which have pleiotropic effects on protein export in Escherichia coli. In this paper, we report the isolation of mutants in which the activity of the secB gene was eliminated...
  52. Fekkes P, de Wit J, van der Wolk J, Kimsey H, Kumamoto C, Driessen A. Preprotein transfer to the Escherichia coli translocase requires the co-operative binding of SecB and the signal sequence to SecA. Mol Microbiol. 1998;29:1179-90 pubmed
    In Escherichia coli, precursor proteins are targeted to the membrane-bound translocase by the cytosolic chaperone SecB. SecB binds to the extreme carboxy-terminus of the SecA ATPase translocase subunit, and this interaction is promoted by ..
  53. Cook H, Kumamoto C. Overproduction of SecA suppresses the export defect caused by a mutation in the gene encoding the Escherichia coli export chaperone secB. J Bacteriol. 1999;181:3010-7 pubmed
    b>SecB is a cytosolic protein required for rapid and efficient export of particular periplasmic and outer membrane proteins in Escherichia coli...
  54. Kumamoto C. Molecular chaperones and protein translocation across the Escherichia coli inner membrane. Mol Microbiol. 1991;5:19-22 pubmed
    ..Two soluble factors, SecB and GroEL, have been implicated in maintenance of the pre-folded conformation and have been termed 'molecular ..
  55. Francetic O, Hanson M, Kumamoto C. prlA suppression of defective export of maltose-binding protein in secB mutants of Escherichia coli. J Bacteriol. 1993;175:4036-44 pubmed
    ..in the periplasmic maltose-binding protein (MBP) (malE18-1) and a point mutation in the soluble export factor SecB (secBL75Q) is completely defective in export of MBP and unable to grow on maltose (Mal- phenotype)...
  56. Kumamoto C, Beckwith J. Mutations in a new gene, secB, cause defective protein localization in Escherichia coli. J Bacteriol. 1983;154:253-60 pubmed
    ..However, the selection also yielded mutants with mutations in a new locus, which was designated secB. These secB mutants were defective in the localization of maltose-binding protein and, in at least one case, OmpF ..
  57. Marrichi M, Camacho L, Russell D, DeLisa M. Genetic toggling of alkaline phosphatase folding reveals signal peptides for all major modes of transport across the inner membrane of bacteria. J Biol Chem. 2008;283:35223-35 pubmed publisher
  58. 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
    b>SecB, a soluble cytosolic chaperone component of the Sec export pathway, binds to newly synthesized precursor proteins and prevents their premature aggregation and folding and subsequently targets them to the translocation machinery on ..
  59. van der Sluis E, Driessen A. Stepwise evolution of the Sec machinery in Proteobacteria. Trends Microbiol. 2006;14:105-8 pubmed
    ..The canonical Sec machinery was initially supplemented with SecB; subsequently, SecE was extended with two transmembrane segments and, finally, SecM was introduced...
  60. Ullers R, Luirink J, Harms N, Schwager F, Georgopoulos C, Genevaux P. SecB is a bona fide generalized chaperone in Escherichia coli. Proc Natl Acad Sci U S A. 2004;101:7583-8 pubmed
    ..Here, we show that the secretion-dedicated chaperone SecB efficiently suppresses both the temperature sensitivity and the aggregation-prone phenotypes of a strain lacking ..
  61. Muller M, Koch H, Beck K, Schafer U. Protein traffic in bacteria: multiple routes from the ribosome to and across the membrane. Prog Nucleic Acid Res Mol Biol. 2001;66:107-57 pubmed
    ..proteins, synthesized as precursors with cleavable signal sequences, require cytoplasmic chaperones, such as SecB, to remain competent for posttranslational transport...
  62. Weiss J, Ray P, Bassford P. Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro. Proc Natl Acad Sci U S A. 1988;85:8978-82 pubmed
    The efficient export of a subset of Escherichia coli envelope proteins is dependent upon the product of the secB gene...
  63. Smith V, Schwartz B, Randall L, Smith R. Electrospray mass spectrometric investigation of the chaperone SecB. Protein Sci. 1996;5:488-94 pubmed
    ..ionization mass spectrometry was used to investigate the structure of the Escherichia coli chaperone protein SecB. It was determined that the N-terminal methionine of SecB has been removed and that more than half of all SecB ..
  64. Peterson J, Woolhead C, Bernstein H. Basic amino acids in a distinct subset of signal peptides promote interaction with the signal recognition particle. J Biol Chem. 2003;278:46155-62 pubmed
    ..Whereas both proteins are normally targeted to the inner membrane by SecB, we found that replacement of their native signal peptides with another moderately hydrophobic but unusually basic ..
  65. Randall L, Hardy S. SecB, one small chaperone in the complex milieu of the cell. Cell Mol Life Sci. 2002;59:1617-23 pubmed
    b>SecB is only one of a plethora of cytosolic chaperones in E. coli whose common property is that they bind nonnative proteins...
  66. Schmidt M, Rollo E, Grodberg J, Oliver D. Nucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli. J Bacteriol. 1988;170:3404-14 pubmed
    ..This and additional evidence are presented indicating that gene X and secA are cotranscribed. ..
  67. Randall L, Hardy S, Topping T, Smith V, Bruce J, Smith R. The interaction between the chaperone SecB and its ligands: evidence for multiple subsites for binding. Protein Sci. 1998;7:2384-90 pubmed
    The chaperone protein SecB is dedicated to the facilitation of export of proteins from the cytoplasm to the periplasm and outer membrane of Escherichia coli...
  68. Zhou J, Xu Z. Structural determinants of SecB recognition by SecA in bacterial protein translocation. Nat Struct Biol. 2003;10:942-7 pubmed publisher
    b>SecB is a bacterial chaperone involved in directing pre-protein to the translocation pathway by its specific interaction with the peripheral membrane ATPase SecA...
  69. Kim J, Luirink J, Kendall D. SecB dependence of an exported protein is a continuum influenced by the characteristics of the signal peptide or early mature region. J Bacteriol. 2000;182:4108-12 pubmed
    ..and the early mature region), the efficiency with which this protein is transported, and its requirement for SecB to accomplish the transport process...
  70. Collier D, Bankaitis V, Weiss J, Bassford P. The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein. Cell. 1988;53:273-83 pubmed
    Evidence is presented that the E. coli secB gene encodes a soluble protein that interacts with the mature region of the precursor maltose-binding protein (MBP), and promotes MBP export by preventing premature folding of the newly ..