HSP33 in eukaryotes - An evolutionary tale of a chaperone adapted to photosynthetic organisms

Na'ama Segal, Michal Shapira

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


Summary HSP33 was originally identified in bacteria as a redox-sensitive chaperone that protects unfolded proteins from aggregation. Here, we describe a eukaryote ortholog of HSP33 from the green algae Chlamydomonas reinhardtii, which appears to play a protective role under light-induced oxidizing conditions. The algal HSP33 exhibits chaperone activity, as shown by citrate synthase aggregation assays. Studies from the Jakob laboratory established that activation of the bacterial HSP33 upon its oxidation initiates by the release of pre-bound Zn from the well conserved Zn-binding motif Cys-X-Cys-Xn-Cys-X-X-Cys, and is followed by significant structural changes (Reichmann et al.,). Unlike the bacterial protein, the HSP33 from C. reinhardtii had lost the first cysteine residue of its center, diminishing Zn-binding activity under all conditions. As a result, the algal protein can be easily activated by minor structural changes in response to oxidation and/or excess heat. An attempt to restore the missing first cysteine did not have a major effect on Zn-binding and on the mode of activation. Replacement of all remaining cysteines abolished completely any residual Zn binding, although the chaperone activation was maintained. A phylogenetic analysis of the algal HSP33 showed that it clusters with the cyanobacterial protein, in line with its biochemical localization to the chloroplast. Indeed, expression of the algal HSP33 increases in response to light-induced oxidative stress, which is experienced routinely by photosynthetic organisms. Despite the fact that no ortholog could be found in higher eukaryotes, its abundance in all algal species examined could have a biotechnological relevance. Significance StatementHsp33 is the only known chaperone which is activated under oxidizing conditions, and was well characterized in bacteria. Since the natural physiology of photosynthetic organisms involves light-induced oxidative stress, we were interested to see whether the algal ortholog, HSP33, is expressed in the chloroplast and if it possesses a similar activation mode. Our results highlight a significant evolutionary variability of the algal protein and we also discuss its biotechnological value.

Original languageEnglish
Pages (from-to)850-860
Number of pages11
JournalPlant Journal
Issue number5
StatePublished - 1 Jun 2015


  • Chlamydomonas reinhardtii
  • HSP33
  • chaperone
  • oxidative stress
  • redox regulation

ASJC Scopus subject areas

  • Genetics
  • Plant Science
  • Cell Biology


Dive into the research topics of 'HSP33 in eukaryotes - An evolutionary tale of a chaperone adapted to photosynthetic organisms'. Together they form a unique fingerprint.

Cite this