Chaperone-like activities of the CsaA protein of Bacillus subtilis.
The growth and protein export defects of Escherichia coli secA51(Ts) strains can be suppressed by the CsaA protein of Bacillus subtilis. The present studies indicate that this effect can be attributed to chaperone-like activities of CsaA. First, CsaA stimulated protein export in secB, groES and dnaJ mutant strains of E. coli. Second, CsaA suppressed the growth defects of dnaK, dnaJ and grpE mutants of E. coli. Third, and most importantly, CsaA exhibited chaperone-like properties by stimulating the reactivation of heat-denatured firefly luciferase in groEL, groES, dnaK and grpE mutant strains of E. coli, and by preventing the aggregation of heat-denatured luciferase in vitro. Thus, it seems that CsaA suppresses the growth and secretion defects of E. coli secA(Ts) strains either by improving the translocation competence of exported pre-proteins, thereby making them better substrates for mutant SecA proteins, or by stimulating the translocation activity of mutant SecA proteins.
Müller
Jörg P
JP
Institute for Molecular Biology, Jena University, Winzerlaer Strasse 10, 07745 Jena, Germany1.
Bron
Sierd
S
Department of Genetics, Center for Biological Sciences, Kerklaan 30, 9751 NN Haren, The Netherlands2.
Venema
Gerard
G
Department of Genetics, Center for Biological Sciences, Kerklaan 30, 9751 NN Haren, The Netherlands2.
Maarten van Dijl
Jan
J
Department of Pharmaceutical Biology, Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands3.
D000251:Adenosine Triphosphatases / Q000235:genetics / Q000378:metabolism; D001412:Bacillus subtilis / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D001692:Biological Transport; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism; D018835:Chaperonin 10 / Q000235:genetics / Q000378:metabolism; D018834:Chaperonin 60 / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000254:growth & development / Q000378:metabolism; D029968:Escherichia coli Proteins; D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism; D008156:Luciferases / Q000378:metabolism; D026901:Membrane Transport Proteins; D018832:Molecular Chaperones / Q000378:metabolism*; D000069816:SEC Translocation Channels; D000081416:SecA Proteins; D013696:Temperature; D014169:Transformation, Bacterial; D001618:beta-Lactamases / Q000378:metabolism
D001426:Bacterial Proteins; D002352:Carrier Proteins; D018835:Chaperonin 10; D018834:Chaperonin 60; C494635:DnaJ protein, E coli; D029968:Escherichia coli Proteins; C068113:GrpE protein, Bacteria; C489400:GrpE protein, E coli; D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D026901:Membrane Transport Proteins; D018832:Molecular Chaperones; D000069816:SEC Translocation Channels; C057842:SecB protein, Bacteria; C077891:CsaA protein, Bacillus subtilis; D008156:Luciferases; D001618:beta-Lactamases; D000251:Adenosine Triphosphatases; C063842:dnaK protein, E coli; D000081416:SecA Proteins