Plant Molecular Biology

, 69:227

Cpn20: Siamese twins of the chaperonin world

  • Celeste Weiss
  • Anat Bonshtien
  • Odelia Farchi-Pisanty
  • Anna Vitlin
  • Abdussalam Azem
Review Article

DOI: 10.1007/s11103-008-9432-3

Cite this article as:
Weiss, C., Bonshtien, A., Farchi-Pisanty, O. et al. Plant Mol Biol (2009) 69: 227. doi:10.1007/s11103-008-9432-3

Abstract

The chloroplast cpn20 protein is a functional homolog of the cpn10 co-chaperonin, but its gene consists of two cpn10-like units joined head-to-tail by a short chain of amino acids. This double protein is unique to plastids and was shown to exist in plants as well plastid-containing parasites. In vitro assays showed that this cpn20 co-chaperonin is a functional homolog of cpn10. In terms of structure, existing data indicate that the oligomer is tetrameric, yet it interacts with a heptameric cpn60 partner. Thus, the functional oligomeric structure remains a mystery. In this review, we summarize what is known about this distinctive chaperonin and use a bioinformatics approach to examine the expression of cpn20 in Arabidopsis thaliana relative to other chaperonin genes in this species. In addition, we examine the primary structure of the two homologous domains for similarities and differences, in comparison with cpn10 from other species. Lastly, we hypothesize as to the oligomeric structure and raison d’être of this unusual co-chaperonin homolog.

Keywords

Chaperonin Cpn10 Cpn20 Cpn21 Protein folding 

Supplementary material

11103_2008_9432_MOESM1_ESM.doc (34 kb)
MOESM1 (DOC 34 kb)

Copyright information

© Springer Science+Business Media B.V. 2008

Authors and Affiliations

  • Celeste Weiss
    • 1
  • Anat Bonshtien
    • 1
  • Odelia Farchi-Pisanty
    • 2
  • Anna Vitlin
    • 1
  • Abdussalam Azem
    • 1
  1. 1.George Wise Faculty of Life Sciences, Department of BiochemistryTel Aviv UniversityTel AvivIsrael
  2. 2.Department of Plant SciencesTel Aviv UniversityTel AvivIsrael

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