The truncated form of the bacterial heat shock protein ClpB/HSP100 contributes to development of thermotolerance in the cyanobacterium Synechococcus sp strain PCC 7942

ClpB is a highly conserved heat shock protein that is essential for thermot olerance in bacteria and eukaryotes. One distinctive feature of all bacteri al clpB genes is the dual translation of a truncated 79-kDa form (ClpB-79) in addition to the full-length 93-kDa protein (ClpB-93). To investigate the currently unknown function of ClpB-79, we have examined the ability of the two different-sized ClpB homologues from the cyanobacterium Synechococcus sp. strain PCC 7942 to confer thermotolerance. We show that the ClpB-79 for m has the same capacity as ClpB-93 to confer thermotolerance and that the C lpB-79 protein contributes ca. one-third of the total thermotolerance devel oped in wild-type Synechococcus, the first in vivo demonstration of a funct ional role for ClpB-79 in bacteria.