Cpn20: Siamese twins of the chaperonin world |
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Authors: | Celeste Weiss Anat Bonshtien Odelia Farchi-Pisanty Anna Vitlin Abdussalam Azem |
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Affiliation: | (1) George Wise Faculty of Life Sciences, Department of Biochemistry, Tel Aviv University, Tel Aviv, Israel;(2) Department of Plant Sciences, Tel Aviv University, Tel Aviv, Israel |
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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. Electronic supplementary material The online version of this article (doi:) contains supplementary material, which is available to authorized users. |
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Keywords: | Chaperonin Cpn10 Cpn20 Cpn21 Protein folding |
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