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PMID: 10816431 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Interaction of Bacillus subtilis CsaA with SecA and precursor proteins.

The Biochemical journal ·Vol. 348 Pt 2 ·2000-06-01 ·Pages 367-73

Müller JP, Ozegowski J, Vettermann S, Swaving J, Van Wely KH, Driessen AJ

Abstract

CsaA from the Gram-positive bacterium Bacillus subtilis has been identified previously as a suppressor of the growth and protein-export defect of Escherichia coli secA(Ts) mutants. CsaA has chaperone-like activities in vivo and in vitro. To examine the role of CsaA in protein export in B. subtilis, expression of the csaA gene was repressed. While export of most proteins remained unaffected, export of at least two proteins was significantly reduced upon CsaA depletion. CsaA co-immunoprecipitates and co-purifies with the SecA proteins of E. coli and B. subtilis, and binds the B. subtilis preprotein prePhoB. Purified CsaA stimulates the translocation of prePhoB into E. coli membrane vesicles bearing the B. subtilis translocase, whereas it interferes with the SecB-mediated translocation of proOmpA into membrane vesicles of E. coli. The specific interaction with the SecA translocation ATPase and preproteins suggests that CsaA acts as a chaperone that promotes the export of a subset of preproteins in B. subtilis.

MeSH Terms
Adenosine Triphosphatases/isolation & purification,metabolism Bacillus subtilis/genetics,metabolism Bacterial Proteins/genetics,isolation & purification,metabolism Carrier Proteins/isolation & purification,metabolism DNA-Binding Proteins/isolation & purification,metabolism Escherichia coli/genetics,metabolism Escherichia coli Proteins Genotype Membrane Transport Proteins Molecular Chaperones Phenotype Plasmids Protein Binding Protein Precursors/isolation & purification,metabolism Recombinant Proteins/isolation & purification,metabolism SEC Translocation Channels SecA Proteins
Chemicals
Bacterial Proteins Carrier Proteins DNA-Binding Proteins Escherichia coli Proteins Membrane Transport Proteins Molecular Chaperones Protein Precursors Recombinant Proteins SEC Translocation Channels PhoB protein, Bacteria CsaA protein, Bacillus subtilis Adenosine Triphosphatases SecA Proteins
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Müller J P
Institute for Molecular Biology, Jena University, Winzerlaer Strasse 10, D-07745 Jena, Germany. jmueller@imb-jena.de
Ozegowski J
Vettermann S
Swaving J
Van Wely K H
Driessen A J
References (47)
47 references, click to expand
  1. Characterization of a Bacillus subtilis SecA mutant protein deficient in translocation ATPase and release from the membrane.
    Mol Microbiol. 1993 Apr;8(1):31-42 PMID: 8497195
  2. Highly selective binding of nascent polypeptides by an Escherichia coli chaperone protein in vivo.
    J Bacteriol. 1993 Apr;175(8):2184-8 PMID: 8468278
  3. Cloning and characterization of a Bacillus subtilis gene encoding a homolog of the 54-kilodalton subunit of mammalian signal recognition particle and Escherichia coli Ffh.
    J Bacteriol. 1993 Aug;175(15):4885-94 PMID: 8335643
  4. Identification of a soluble SecA/SecB complex by means of a subfractionated cell-free export system.
    J Biol Chem. 1994 Apr 29;269(17):12833-9 PMID: 8175697
  5. High selectivity with low specificity: how SecB has solved the paradox of chaperone binding.
    Trends Biochem Sci. 1995 Feb;20(2):65-9 PMID: 7701564
  6. SecYEG and SecA are the stoichiometric components of preprotein translocase.
    J Biol Chem. 1995 Aug 25;270(34):20106-11 PMID: 7650029
  7. Overproduction, purification and characterization of GroES and GroEL from thermophilic Bacillus stearothermophilus.
    FEMS Microbiol Lett. 1995 Dec 15;134(2-3):183-8 PMID: 8586266
  8. SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF.
    Cell. 1995 Dec 29;83(7):1171-81 PMID: 8548804
  9. Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli.
    J Bacteriol. 1996 Jun;178(12):3608-13 PMID: 8655561
  10. SecA is an intrinsic subunit of the Escherichia coli preprotein translocase and exposes its carboxyl terminus to the periplasm.
    Mol Microbiol. 1996 Nov;22(4):619-29 PMID: 8951810
  11. The chemistry and enzymology of the type I signal peptidases.
    Protein Sci. 1997 Jun;6(6):1129-38 PMID: 9194173
  12. The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation.
    EMBO J. 1997 Oct 15;16(20):6105-13 PMID: 9321390
  13. The complete genome sequence of the gram-positive bacterium Bacillus subtilis.
    Nature. 1997 Nov 20;390(6657):249-56 PMID: 9384377
  14. Interaction between SecA and SecYEG in micellar solution and formation of the membrane-inserted state.
    Biochemistry. 1998 Jan 6;37(1):201-10 PMID: 9425040
  15. Protein secretion in phosphate-limited cultures of Bacillus subtilis 168.
    Appl Microbiol Biotechnol. 1998 Mar;49(3):321-7 PMID: 9581295
  16. Translocation of the precursor of alpha-amylase into Bacillus subtilis membrane vesicles.
    Eur J Biochem. 1998 Aug 1;255(3):690-7 PMID: 9738909
  17. A vector for systematic gene inactivation in Bacillus subtilis.
    Microbiology. 1998 Nov;144 ( Pt 11):3097-104 PMID: 9846745
  18. Enhancing effect of Bacillus subtilis Ffh, a homologue of the SRP54 subunit of the mammalian signal recognition particle, on the binding of SecA to precursors of secretory proteins in vitro.
    J Biochem. 1999 Jan;125(1):151-9 PMID: 9880811
  19. Protein targeting to the bacterial cytoplasmic membrane.
    Microbiol Mol Biol Rev. 1999 Mar;63(1):161-73 PMID: 10066835
  20. Improving protein secretion by engineering components of the bacterial translocation machinery.
    Curr Opin Biotechnol. 1999 Aug;10(4):376-81 PMID: 10449317
  21. Preprotein translocation by a hybrid translocase composed of Escherichia coli and Bacillus subtilis subunits.
    J Bacteriol. 1999 Nov;181(22):7021-7 PMID: 10559168
  22. Chaperone-like activities of the CsaA protein of Bacillus subtilis.
    Microbiology. 2000 Jan;146 ( Pt 1):77-88 PMID: 10658654
  23. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
    Nature. 1970 Aug 15;227(5259):680-5 PMID: 5432063
  24. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.
    Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350-4 PMID: 388439
  25. Regulation of a membrane component required for protein secretion in Escherichia coli.
    Cell. 1982 Aug;30(1):311-9 PMID: 6751561
  26. Construction of a Bacillus subtilis double mutant deficient in extracellular alkaline and neutral proteases.
    J Bacteriol. 1984 Oct;160(1):442-4 PMID: 6434524
  27. Evidence for specificity at an early step in protein export in Escherichia coli.
    J Bacteriol. 1985 Jul;163(1):267-74 PMID: 3891730
  28. Improved oligonucleotide site-directed mutagenesis using M13 vectors.
    Nucleic Acids Res. 1985 Jun 25;13(12):4431-43 PMID: 2989795
  29. Leader peptidase catalyzes the release of exported proteins from the outer surface of the Escherichia coli plasma membrane.
    J Biol Chem. 1985 Dec 15;260(29):15925-31 PMID: 2999144
  30. SecA protein is required for secretory protein translocation into E. coli membrane vesicles.
    Cell. 1988 Nov 18;55(4):683-92 PMID: 2846186
  31. 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 Dec;85(23):8978-82 PMID: 2848249
  32. Characterization of the Escherichia coli protein-export gene secB.
    Gene. 1989 Jan 30;75(1):167-75 PMID: 2656409
  33. Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli.
    EMBO J. 1989 Nov;8(11):3517-21 PMID: 2573517
  34. Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form soluble complexes with precursor proteins in vitro.
    EMBO J. 1989 Sep;8(9):2703-9 PMID: 2531087
  35. In vivo degradation of secreted fusion proteins by the Escherichia coli outer membrane protease OmpT.
    J Bacteriol. 1990 Jan;172(1):491-4 PMID: 2403549
  36. Evidence for two structural genes for alkaline phosphatase in Bacillus subtilis.
    J Bacteriol. 1990 Feb;172(2):735-40 PMID: 2105301
  37. The signal peptide.
    J Membr Biol. 1990 May;115(3):195-201 PMID: 2197415
  38. The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane.
    Cell. 1990 Oct 19;63(2):269-79 PMID: 2170023
  39. The secD locus of E.coli codes for two membrane proteins required for protein export.
    EMBO J. 1990 Oct;9(10):3209-16 PMID: 2170107
  40. Heat-shock proteins can substitute for SecB function during protein export in Escherichia coli.
    EMBO J. 1991 Feb;10(2):239-45 PMID: 1671351
  41. Signal peptidase I overproduction results in increased efficiencies of export and maturation of hybrid secretory proteins in Escherichia coli.
    Mol Gen Genet. 1991 May;227(1):40-8 PMID: 1904537
  42. The enzymology of protein translocation across the Escherichia coli plasma membrane.
    Annu Rev Biochem. 1991;60:101-24 PMID: 1831965
  43. Small cytoplasmic RNA of Bacillus subtilis: functional relationship with human signal recognition particle 7S RNA and Escherichia coli 4.5S RNA.
    J Bacteriol. 1992 Apr;174(7):2185-92 PMID: 1372600
  44. DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli.
    Genes Dev. 1992 Jul;6(7):1165-72 PMID: 1628824
  45. Suppression of the growth and export defects of an Escherichia coli secA(Ts) mutant by a gene cloned from Bacillus subtilis.
    Mol Gen Genet. 1992 Oct;235(1):89-96 PMID: 1435734
  46. The E. coli ffh gene is necessary for viability and efficient protein export.
    Nature. 1992 Oct 22;359(6397):744-6 PMID: 1331806
  47. Accumulation of secretory protein precursors in Escherichia coli induces the heat shock response.
    J Bacteriol. 1993 Jul;175(13):3992-7 PMID: 8320215
Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
2000-06-01
Pages
367-73
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1221075
Subset
IM
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