Environment and Biotechnology Centre, Faculty of Life and Social Sciences, Swinburne University of Technology, P.O. Box 218, Hawthorn, VIC 3122, Australia.
FEBS Lett. 2012 Oct 19;586(20):3539-47. doi: 10.1016/j.febslet.2012.09.002. Epub 2012 Sep 13.
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.
FK506 结合蛋白（FKBP）既是免疫抑制剂药物的受体，也是催化脯氨酸键旋转的脯氨酰异构酶（PPIase）酶。FKBP 的特征是包含至少一个 FK506 结合结构域（FKBd），这是脯氨酸的受体位点和 PPIase 催化的活性位点。FKBP 在大多数生物体中形成庞大而多样的家族，其中最大的 FKBP 家族存在于高等植物中。植物 FKBP 是分子伴侣，与特定的蛋白质伙伴相互作用，调节多种细胞过程。最近的研究发现，植物 FKBP 以复杂和协调的机制运作，以调节应激反应和发育过程，并且发现新的相互作用伙伴将它们的细胞影响扩展到基因表达和光合作用适应。本综述在这些最新发现的背景下，检查了高等植物 FKBP 家族的分子和结构特征以及功能作用，并讨论了结构域保守性和变异性对于形成多样化、多功能和复杂伴侣家族的意义。
