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Journal of Bacteriology, December 2001, p. 7381-7386, Vol. 183, No. 24
Philipps-Universität Marburg, FB
Chemie, D-35032 Marburg, Germany
Received 2 July 2001/Accepted 14 September 2001
The cold shock response in both Escherichia coli and
Bacillus subtilis is induced by an abrupt downshift in
growth temperature and leads to a dramatic increase in the production
of a homologous class of small, often highly acidic cold shock
proteins. This protein family is the prototype of the cold shock domain
(CSD) that is conserved from bacteria to humans. For B. subtilis it has been shown that at least one of the three
resident cold shock proteins (CspB to D) is essential under optimal
growth conditions as well as during cold shock. Analysis of the
B. subtilis cspB cspC double deletion mutant revealed that
removal of these csp genes results in pleiotropic
alteration of protein synthesis, cell lysis during the entry of
stationary growth phase, and the inability to differentiate into
endospores. We show here that heterologous expression of the
translation initiation factor IF1 from E. coli in a
B. subtilis cspB cspC double deletion strain is able to
cure both the growth and the sporulation defects observed for this
mutant, suggesting that IF1 and cold shock proteins have at least in
part overlapping cellular function(s). Two of the possible explanation
models are discussed.
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.24.7381-7386.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Complementation of Cold Shock Proteins by
Translation Initiation Factor IF1 In Vivo
*
Corresponding author. Mailing address:
Philipps-Universität Marburg, FB Chemie, Hans-Meerwein-Str.,
D-35032 Marburg, Germany. Phone: 49 6421-28-25722. Fax: 49 6421-28-22191. E-mail: marahiel{at}chemie.uni-marburg.de.
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