Identification of DnaJ-like chaperone in Clostridium botulinum type A

H. D. Shukla, B. R. Singh

Research output: Contribution to journalArticle

Abstract

Clostridium botulinum type A cells, when challenged to elevated temperature (45°C), increased the expression of at least nine heat shock proteins (HSPs). Simultaneously with the induction of HSPs, changes in the synthesis rates of other cellular proteins were observed. A 40-kDa stress protein was induced and its synthesis rate was enhanced when the cells were shifted to 45°C. Using heterologous antibodies raised against E. coli DnaJ heat shock proteins, the 40-kDa stress protein of C. botulinum type A has been identified as a DnaJ-like chaperone. The DnaJ chaperone might be involved in translocation of the neurotoxin and other cellular proteins across the cell membrane, repair of damaged proteins, and organism survival inside the host. This is the first report of the existence of a DnaJ-like chaperone in this organism.

Original languageEnglish (US)
Pages (from-to)695-700
Number of pages6
JournalJournal of Protein Chemistry
Volume18
Issue number6
DOIs
StatePublished - Jan 1 1999

Keywords

  • Chaperone
  • DnaJ
  • Heat shock proteins
  • Neurotoxin
  • Neurotoxin complex
  • Translocation

ASJC Scopus subject areas

  • Biochemistry

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