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Journal of Bacteriology, October 1998, p. 5173-5182, Vol. 180, No. 19
Department of Plant Sciences, University of
Western Ontario, London, Ontario, Canada N6A 5B7
Received 6 February 1998/Accepted 30 April 1998
The sequence of a genomic clone encoding a 100-kDa stress protein
of Plectonema boryanum (p-ClpB) was determined.
The predicted polypeptide contains two putative ATPase regions located
within two highly conserved domains (N1 and N2), a spacer region that likely forms a coiled-coil domain, and a highly conserved consensus CK2
phosphorylation domain. The coiled-coil region and the putative site of
phosphorylation are not unique to p-ClpB; they are present in all ClpB sequences examined and are absent from the ClpB paralogs ClpA, ClpC, ClpX, and ClpY. Small quantities of a 4.5-kb
p-clpB transcript and 110-kDa cytosolic p-ClpB
protein were detected in cells grown under optimal conditions; however,
increases in the quantities of the transcript and protein were observed
in cells grown under excess light and low temperature conditions. Finally, we analyzed ClpA, ClpB, and ClpC sequences from 27 organisms in order to predict phylogenetic relationships among the homologs. We
have used this information, along with an identity alignment, to
redefine the Clp subfamilies.
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
ClpB in a Cyanobacterium: Predicted Structure,
Phylogenetic Relationships, and Regulation by Light and
Temperature
,*

*
Corresponding author. Mailing address: Department of
Biology, Indiana University, Jordan Hall, Bloomington, IN 47405. Phone: (812) 855-3692. Fax: (812) 855-6705. E-mail:
mcelerin{at}sunflower.bio.indiana.edu.
Present address: Department of Biology, Indiana University,
Bloomington, IN 47405.
Present address: Department of Botany, University of Toronto,
Toronto, Ontario, Canada M5S 1A1.
§
Present address: Institute of Biophysics, Bulgarian Academy of
Sciences, 1113 Sofia, Bulgaria.
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