@article{clarke_truncated_2000,
	title = {The {Truncated} {Form} of the {Bacterial} {Heat} {Shock} {Protein}  {ClpB}/{HSP100} {Contributes} to {Development} of {Thermotolerance}  in the {Cyanobacterium} {Synechococcus} sp. {Strain} {PCC} 7942},
	volume = {182},
	issn = {0021-9193},
	url = {https://www.ncbi.nlm.nih.gov/pmc/articles/PMC94841/},
	abstract = {ClpB is a highly conserved heat shock protein that is essential for thermotolerance in bacteria and eukaryotes. One distinctive feature of all bacterial 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 form has the same capacity as ClpB-93 to confer thermotolerance and that the ClpB-79 protein contributes ca. one-third of the total thermotolerance developed in wild-type Synechococcus, the first in vivo demonstration of a functional role for ClpB-79 in bacteria.},
	number = {24},
	urldate = {2021-11-08},
	journal = {Journal of Bacteriology},
	author = {Clarke, Adrian K. and Eriksson, Mats-Jerry},
	month = dec,
	year = {2000},
	pmid = {11092876},
	pmcid = {PMC94841},
	pages = {7092--7096},
}

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