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J Biol Chem, Vol. 274, Issue 6, 3407-3413, February 5, 1999

The Family of Cold Shock Proteins of Bacillus subtilis
STABILITY AND DYNAMICS IN VITRO AND IN VIVO

Thomas Schindler, Peter L. Graumann, Dieter Perl, Saufung Ma, Franz X. Schmid, and Mohamed A. Marahiel

From the  Laboratorium für Biochemie, Universität Bayreuth, 95440 Bayreuth and the  Biochemie, Fachbereich Chemie, Hans-Meerwein-Strasse, Philipps-Universität Marburg, 35032 Marburg, Germany

Bacillus subtilis possesses three homologous small cold shock proteins (CSPs; CspB, CspC, CspD, sequence identity >72%). They share a similar -sheet structure, as shown by circular dichroism, and have a very low conformational stability, with CspC being the least stable. Similar to CspB, CspC and CspD unfold and refold extremely fast in a N  U two-state reaction with average lifetimes of only 100-150 ms for the native state and 1-6 ms for the unfolded states at 25 °C. As a consequence of their low stability and low kinetic protection against unfolding, all three cold shock proteins are rapidly degraded by proteases in vitro. Analysis of the CSP stabilities in vivo by pulse-chase experiments revealed that CspB and CspD are stable during logarithmic growth at 37 °C as well as after cold shock. The cellular half-life of CspC is shortened at 37 °C, but under cold shock conditions CspC becomes stable. The proteolytic susceptibility of the CSPs in vitro was strongly reduced in the presence of a nucleic acid ligand, suggesting that the observed stabilization of CSPs in vivo is mediated by binding to their substrate mRNA at 37 °C and, in particular, under cold shock conditions.

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