PPIase activities and interaction partners of FK506-binding proteins in the wheat thylakoid

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Title: PPIase activities and interaction partners of FK506-binding proteins in the wheat thylakoid
Author(s): Gollan, Peter J.; Ziemann, Mark; Bhave, Mrinal
Abstract: FK506-binding proteins (FKBPs) and cyclophilins, collectively called immunophilins, conserve peptidyl-prolyl cis/trans isomerase (PPIase) active sites, although many lack PPIase activity. The chloroplast thylakoid contains a large proportion of the plant immunophilin family, but their functions within this compartment are unclear. Some lumenal immunophilins are important for assembly of photosynthetic complexes, implicating them in the maintenance and turnover of the photosynthetic apparatus during acclimation processes. In this investigation into the functions of three FKBPs localized to the thylakoid of Triticum aestivum (wheat), we present the first evidence of PPIase activity in the thylakoid of a cereal plant, and also show that PPIase activity is not conserved in all lumenal FKBPs. Using yeast two-hybrid analysis we found that the PPIase-active FKBP13 interacts with the globular domain of the wheat Rieske protein, with potential impact on photosynthetic electron transfer. Specific interaction partners for PPIase-deficient FKBP16-1 and FKBP16-3 link these isoforms to photosystem assembly.
Publication type: Journal article
Research centre: Swinburne University of Technology. Faculty of Life and Social Sciences. Environment and Biotechnology Centre
Source: Physiologia Plantarum, Vol. 143, no. 4 (Dec 2011), pp. 385-395
Publication year: 2011
FOR Code(s): 0601 Biochemistry and Cell Biology; 060407 Genome Structure and Regulation; 0607 Plant Biology; 060702 Plant Cell and Molecular Biology; 060704 Plant Pathology; 0706 Horticultural Production
Keyword(s): Cereal plants; FK506-binding proteins; FKBPs; PPIase activites; Proteins; Thylakoids; Triticum aestivum; Wheat
Publisher: Wiley-Blackwell Publishing
ISSN: 0031-9317
Publisher URL: http://dx.doi.org/10.1111/j.1399-3054.2011.01503.x
Peer reviewed