The FKBP families of higher plants: exploring the structures and functions of protein interaction specialists

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Bhave, Mrinal

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The FKBP families of higher plants: exploring the structures and functions of protein interaction specialists

Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.3/235670

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Title: The FKBP families of higher plants: exploring the structures and functions of protein interaction specialists
Author(s): Gollan, Peter J.; Bhave, Mrinal; Aro, Eva-Mari
Abstract: The FK506-binding proteins (FKBPs) are known both as the receptors for immunosuppressant drugs and as prolyl isomerase (PPIase) enzymes that catalyse rotation of prolyl bonds. FKBPs are characterised by the inclusion of at least one FK506-binding domain (FKBd), the receptor site for proline and the active site for PPIase catalysis. The FKBPs form large and diverse families in most organisms, with the largest FKBP families occurring in higher plants. Plant FKBPs are molecular chaperones that interact with specific protein partners to regulate a diversity of cellular processes. Recent studies have found that plant FKBPs operate in intricate and coordinated mechanisms for regulating stress response and development processes, and discoveries of new interaction partners expand their cellular influences to gene expression and photosynthetic adaptations. This review presents an examination of the molecular and structural features and functional roles of the higher plant FKBP family within the context of these recent findings, and discusses the significance of domain conservation and variation for the development of a diverse, versatile and complex chaperone family.
Publication type: Journal article
Research centre: Swinburne University of Technology. Faculty of Life and Social Sciences. Environment and Biotechnology Centre
Source: FEBS Letters, Vol. 586, no. 20 (Oct 2012), pp. 3539-3547
Publication year: 2012
FOR Code(s): 0304 Medicinal and Biomolecular Chemistry; 0601 Biochemistry and Cell Biology
Keyword(s): FK506-binding proteins; Immunophilin; Molecular chaperone; Phosphorylation; Plants; PPIase; Prolyl isomerase; Stress response
Publisher: Elsevier
ISSN: 0014-5793
Publisher URL: http://dx.doi.org/10.1016/j.febslet.2012.09.002
Peer reviewed