Skip to main content
Log in

Molecular characterization of specific heat shock proteins inBacillus subtilis

  • Published:
Current Microbiology Aims and scope Submit manuscript

Abstract

Heat shock inBacillus subtilis may induce as many as 66 proteins after temperature upshift from 37° to 48°C. Four induced proteins were analyzed by microsequencing techniques. These were identified as the homologues for GroEL, DnaK, enolase, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH), which are heat shock proteins in other systems. The identities of GroEL and DnaK were confirmed additionally by Western blot analysis. As a control, a protein whose synthesis was repressed approximately threefold by heat shock was identified by microsequencing as flagellin.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Literature Cited

  1. Albano M, Hahn J, Dubnau D (1987) Expression of competence genes inBacillus subtilis. J Bacteriol 169:3110–3117

    Google Scholar 

  2. Arnosti DN, Singer VL, Chamberlin MJ (1986) Characterization of heat shock inBacillus subtilis. J Bacteriol 168:1243–1249

    Google Scholar 

  3. Bardwell JCA, Craig EA (1984) Major heat shock gene ofDrosophila and theEscherichia coli heat-induciblednaK gene are homologous. Proc Natl Acad Sci USA 81:848–852

    Google Scholar 

  4. Brandant G, Brandant C (1985) Nucleotide sequence of theEscherichia coli gap gene. Different evolutionary behavior of the NAD+-binding domain and of the catalytic domain ofd-glyceraldehyde-3-phosphate dehydrogenase. Eur J Biochem 150:61–66

    Google Scholar 

  5. Carrascosa JL, Garcia JA, Salas M (1982) A protein similar toEscherichia coli groEL is present inBacillus subtilis. J Mol Biol 158:731–737

    Google Scholar 

  6. DeLange RJ, Chang JY, Shaper JH, Glazer AN (1976) Amino acid sequence of flagellin ofBacillus subtilis 168. III. Tryptic peptides,N-bromosuccinimide peptides, and the complete amino acid sequence. J Biol Chem 251:705–711

    Google Scholar 

  7. Doi RC (1989) Sporulation and germination. In Harwood CR (ed), Bacillus. New York: Plenum Press, pp 169–215

    Google Scholar 

  8. Giallongo A, Salvatore F, Moore R, Croce CM, Showe LC (1986) Molecular cloning and nucleotide sequence of a full-length cDNA for human enolase. Proc Natl Acad Sci USA 83:6741–6745

    Google Scholar 

  9. Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, Hendrix RW, Ellis RJ (1988) Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature 333:330–334

    Google Scholar 

  10. Kennedy TE, Gawinowicz MA, Barzilai A, Kandel ER, Sweatt JD (1988) Sequencing of protein from two-dimensional gels by usingin situ digestion and transfer of peptides to polyvinylidene membranes: application to proteins associated with sensitization inAplysia. Proc. Natl Acad Sci USA 85:7008–7012

    Google Scholar 

  11. Kennedy TE, Wager-Smith K, Barzilai ER, Kandel ER, Sweatt JD (1988) Sequencing proteins from acrylamide gels. Nature 336:499–500

    Google Scholar 

  12. Lindquist S (1986) The heat-shock response. Annu Rev Biochem 55:1151–1191

    Google Scholar 

  13. Lindquist S, Craig EA (1988) The heat-shock proteins. Annu Rev Genet 22:631–677

    Google Scholar 

  14. Love PE, Lyle MJ, Yasbin RE (1985) DNA-damage inducible (din) loci are transcriptionally activated in competentBacillus subtilis. Proc Natl Acad Sci USA 82:6201–6205

    Google Scholar 

  15. Neidhardt FC, VanBogelen RA (1987) Heat shock response. In: Neidhardt FC, Ingraham JL, Low KB, Magasanik B, Schaechter M, Umbarger HE (eds)Escherichia coli andSalmonella typhimurium: cellular and molecular biology. Washington, DC: American Society for Microbiology, pp 1334–1345

    Google Scholar 

  16. O'Farrell PH (1975) High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250:4007–4021

    Google Scholar 

  17. Phillips TA (1988) Two-dimensional polyacrylamide gel electrophoresis of proteins. In: Oxender DL (ed), DNA and protein engineering techniques, vol. 1. New York: Alan R. Liss, Inc., pp 5–9

    Google Scholar 

  18. Qoronfleh MW, Streips UN (1987) Initial subcellular localization of heat-shock proteins inBacillus subtilis. FEMS Microbiol Lett 43:373–377

    Google Scholar 

  19. Richter A, Hecker M (1986) Heat-shock proteins inBacillus subtilis: a two-dimensional gel electrophoresis study. FEMS Microbiol Lett 36:69–71

    Google Scholar 

  20. Rochester DE, Winer JA, Shah DM (1986) The structure and expression of maize genes encoding the major heat shock protein. hsp70. EMBO J 5:451–458

    Google Scholar 

  21. Sakimura K, Kushiya E, Obinata M, Odani S, Takahashi Y (1985) Molecular cloning and the nucleotide sequence of cDNA for neuron-specific enolase messenger RNA of rat brain. Proc Natl Acad Sci USA 82:7453–7457

    Google Scholar 

  22. Shinnick TM (1987) The 65-kilodalton antigen ofMycobacterium tuberculosis. J Bacteriol 169:1080–1088

    Google Scholar 

  23. Streips UN, Polio FW (1985) Heat shock proteins in Bacilli. J Bacteriol 162:434–437

    Google Scholar 

  24. Walker JE, Carne AF, Runswick MJ, Bridgen J, Harris JI (1980)d-Glyceraldehyde-3-phosphate dehydrogenase. Complete amino-acid sequence of the enzyme fromBacillus stearothermophilus. Eur J Biochem 108:549–565

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Miller, B.S., Kennedy, T.E. & Streips, U.N. Molecular characterization of specific heat shock proteins inBacillus subtilis . Current Microbiology 22, 231–236 (1991). https://doi.org/10.1007/BF02092314

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF02092314

Keywords

Navigation