Identification of DnaJ-like chaperone in Clostridium botulinum type A.
Clostridium botulinum type A cells, when challenged to elevated temperature (45 degrees 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 degrees 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.
Shukla
H D
HD
Department of Chemistry and Biochemistry, and Center for Marine Science and Technology, University of Massachusetts, Dartmouth 02747, USA.
Singh
B R
BR
D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry*; D015153:Blotting, Western; D003014:Clostridium botulinum / Q000737:chemistry* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D050956:HSP40 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000096:biosynthesis / Q000737:chemistry*; D006358:Hot Temperature
D001426:Bacterial Proteins; D050956:HSP40 Heat-Shock Proteins; D006360:Heat-Shock Proteins